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M G Rossmann

Publications and source records attributed to M G Rossmann.

At least 163 records · Page 9Linked to original sources
PubMed1986

Effect of errors, redundancy, and solvent content in the molecular replacement procedure for the structure determination of biological macromolecules.

The power of molecular replacement as a tool for analyzing macromolecular structures such as viruses has been demonstrated by an increasing number of successful determinations. We examine here the effects of noncrystallographic redundancy, N; the fraction of solvent volume (1- U/V); error in structure amplitude measurements, R; the fraction, f, of the unique data that were measured; error in the description of the noncrystallographic symmetry; and definition of the molecular envelope. The formula P = (Nf)1/2/R(U/V) has been derived and represents the inherent phasing power (P) for a given problem. The ability of "solvent flattening" procedures to determine phases was analyzed and found to be analogous to the effect of noncrystallographic redundancy. However, in the limiting case, the effect of solvent flattening approaches the power of Sayre's equations.

Crystallography↗
PubMed1985

The active center of catalase.

The refined structure of beef liver catalase (I. Fita, A. M. Silva, M. R. N. Murthy & M. G. Rossmann, unpublished results) is here examined with regard to possible catalytic mechanisms. The distal side of the deeply buried heme pocket is connected with the surface of the molecule by one (or possibly two) channel. The electron density representing the heme group, in each of the two crystallographically independent subunits, is consistent with degradation of the porphyrin rings. The heme group appears to be buckled, reflecting the high content of bile pigment in liver catalase. The spatial organization on the proximal side (where the fifth ligand of the iron is located) shows an elaborate network of interactions. The distal side contains the substrate pocket. The limited space in this region severely constrains possible substrate positions and orientations. The N delta atom of the essential His74 residue hydrogen bonds with O gamma of Ser113, which in turn hydrogen bonds to a water molecule associated with the propionic carbonylic group of pyrrole III. These interactions are also visible in the refined structure of Penicillium vitale catalase (B. K. Vainshtein, W. R. Melik-Adamyan, V. V. Barynin, A. A. Vagin, A. I. Grebenko, V. V. Borisov, K. S. Bartels, I. Fita, & M. G. Rossmann, unpublished results). Model building suggests a pathway for a catalase mechanism (compound I formation, as well as catalatic and peroxidatic reactions). There are some similarities in compound I formation of catalase and cytochrome c peroxidase.

Amino Acid Sequence↗
PubMed1985

The structure of a T = 1 icosahedral empty particle from southern bean mosaic virus.

The structure of a T = 1 icosahedral particle (where T is the triangulation number), assembled from southern bean mosaic virus coat protein fragments that lacked the amino-terminal arm, was solved by means of model building procedures with the use of 6-angstrom resolution x-ray diffraction data. The icosahedral five-, three-, and twofold contacts were found to be similar, at this resolution, to the analogous contacts (icosahedral five-, quasi-three-, and quasi-twofolds) found in the parent T = 3 southern bean mosaic virus. However, the icosahedral fivefold contacts of the T = 3 structure are the most conserved in the T = 1 capsid. These results are consistent with a mechanism in which pentameric caps of dimers are the building blocks for the assembly of T = 1 and T = 3 icosahedral viruses.

Capsid↗
PubMed1985

The NADPH binding site on beef liver catalase.

Beef liver and human erythrocyte catalases (EC 1.11.1.6) bind NADP tenaciously [Kirkman, H. N. & Gaetani, G. F. (1984) Proc. Natl. Acad. Sci. USA 81, 4343-4348]. The position of NADP on beef liver catalase corresponds to the carboxyl-terminal polypeptide hinge in Penicillium vitale fungal catalase, which connects the common catalase structure to the additional flavodoxin-like domain. In contrast to nearly all other known structures of protein-bound NADP, NAD, and FAD, the NADP molecule of beef liver catalase is folded into a right-handed helix and bound, in part, in the vicinity of the carboxyl end of two alpha-helices. A water molecule (W7) occupies a pseudosubstrate site close to the C4 position of the nicotinamide and is hydrogen bonded to His-304. Although the NADP and heme groups approach each other to within 13.7 A, there is no direct interaction. The function of the NADP remains a mystery.

Animals↗
PubMed1984

Picornaviruses of two different genera have similar structures.

Crystals of Mengo virus were used to collect three-dimensional X-ray diffraction data to 7 A resolution. A self-rotation function showed the precise orientation of the Mengo particles in the crystal unit cell. A cross-rotation function against similar data of cubic rhinovirus crystals showed a peak when the orientations of these two icosahedral viruses were superimposed. This demonstrates similarity of capsid construction between two picornaviruses of different taxonomic genera.

Crystallization↗
PubMed1984

Constraints on the assembly of spherical virus particles.

Examination of protein structure shows that it is not possible to deform protein domains to the extent required by the Caspar-Klug quasi-symmetry surface lattices for the description of viral capsids (D. L. D. Caspar and A. Klug (1962). Cold Spring Harbor Symp. Quant. Biol. 27, 1-24). However, flexibility in proteins can be achieved by a number of ligand-induced events. One type of alteration is that of quaternary structural changes in oligomers. This strategy has been used by southern bean mosaic virus and tomato bushy stunt virus where dimers attain two different states in the assembled capsid. Alterations of subunit interactions can be induced by association with RNA, cations, or other oligomeric units and, hence, successful assembly results from a stepwise aggregation. The nature of the oligomers (dimers, trimers, or pentamers) must be the underlying reason for the occurrence of the Caspar-Klug lattices and the organization into icosahedra. An analysis of the surface lattices shows which types of oligomers will be necessary for assembly.

Capsid↗
PubMed1983

Structure of a T = 1 aggregate of alfalfa mosaic virus coat protein seen at 4.5 A resolution.

A T = 1 empty aggregate of alfalfa mosaic virus coat protein had been crystallized in a hexagonal unit cell and its orientation was determined with the rotation function. A single heavy-atom derivative has now been prepared and the position of the two Hg atoms per protein subunit were determined using a systematic Patterson search procedure, given the particle orientation. Phases, initially determined by single isomorphous replacement, were refined by six cycles of electron density averaging and solvent leveling to produce a 4.5 A resolution electron density map. The protein coat is confined between 95 and 58 A radius. The subunit boundary could be delineated easily. It has a central cavity reminiscent of the beta-barrel in other spherical plant viruses, but its topology could not be determined unambiguously. The spherical particle has large holes at the 5-fold axes, consistent with previous observations. The subunits have substantial interactions at the 2 and 3-fold axes. The structure of the elongated particles is discussed in relation to these results.

Capsid↗
PubMed1983

Structural comparisons of some small spherical plant viruses.

The structures of tomato bushy stunt virus, southern bean mosaic virus and satellite tobacco necrosis virus have been compared quantitatively. The organization of the shell domains of tomato bushy stunt virus and southern bean mosaic virus within the icosahedral envelope is identical. The wedge-shaped end of the subunit is closer to the fivefold or quasi-sixfold axes in all three viruses but the packing about the three- and twofold axes is quite different in satellite tobacco necrosis virus as compared to tomato bushy stunt virus or southern bean mosaic virus. The polypeptide folds of these viruses have greatest similarity in the beta-sheet region of the eight-stranded anti-parallel beta-barrel. The largest differences occur in the connecting segments. There is no clear indication of homologous amino acid sequences between southern bean mosaic virus and satellite tobacco necrosis virus. However, there is some conservation of the following functional groups. (1) Threonines and serines at the hexagonal-pentagonal wedge-shaped end of the subunit. (2) Lysines and arginines at the protein-RNA interface. (3) Hydrophobic residues in the cavity within the anti-parallel beta-barrel. (4) An aspartic acid near a site which binds Ca in tomato bushy stunt virus. (5) Ionic interactions in the contacts between fivefold-related subunits. These virus coat protein structures are not as similar to each other as the alpha and beta chains of hemoglobin but have greater likeness to one another than the NAD-binding domains of dehydrogenases or lysozymes from hen egg-white and T4 phage. The surface domains of tomato bushy stunt virus and southern bean mosaic virus are more like each other than like satellite tobacco necrosis virus. A divergent evolutionary tree is proposed on the basis of these observations.

Amino Acids↗
PubMed1983

Crystallization of a common cold virus, human rhinovirus 14: "isomorphism" with poliovirus crystals.

Crystals of rhinovirus 14 have been grown reproducibly. They diffract x-rays to a resolution of at least 3.5 A. The orthorhombic crystal unit cell contains two virions, each situated on a crystallographic twofold axis. At less than 30-A resolution, the space group approximates to 1222 with the particles possessing 222 pseudo crystallographic symmetry. The crystals are "isomorphous" with type I polio crystals [Finch, J. T. & Klug, A. (1959) Nature (London) 183, 1709-1714; Hogle, J. M. (1982) J. Mol. Biol. 160, 663-668], suggesting some similarities of structure between enteroviruses and rhinoviruses.

Crystallization↗
PubMed1983

RNA-protein interactions in some small plant viruses.

The structure of the three quasi-equivalent protein subunits A, B and C of the spherical, T = 3 southern bean mosaic virus (SBMV) have been carefully built in accordance with a refined electron density map of the complete virus. The lower electron density in the RNA portion of the map could not be explicitly interpreted in terms of a preferred RNA structure on which some icosahedral symmetry might have been imposed. However, the extremely basic nature of the interior surface of the coat protein must be associated with the binding and organization of the RNA. Comparison with the small spherical, T = 1 satellite tobacco necrosis virus (STNV; Liljas et al., J. Mol. Biol. 159, 93-108, 1982) and the T = 1 aggregate of alfalfa mosaic virus (AMV) protein (Fukuyama et al., J. Mol. Biol. 150, 33-41, 1981) showed similar results. The pattern of basic residues on the SBMV coat protein surface facing the RNA is able to dock a 9 base pair double-helical A-RNA structure with surprising accuracy. The basic residues are each associated with a different phosphate and the protein can make interactions with five bases in the minor groove. This may be one of a small number of ways in which the RNA interacts with SBMV coat protein. The self-assembly of SBMV has been studied in relation to the presence of the 63 basic amino-terminal coat protein sequence, pH, Ca2+ and Mg2+ ions and RNA. These results have led to a two-state model where the "relaxed" dimers initially self-assemble into 10-mer caps which nucleate the assembly of T = 1 or T = 3 capsids depending on the charge state of the carboxyl group clusters in the subunit contact region. The two-state condition of dimers in a viral coat protein extends the range of structures originally envisaged by Caspar and Klug (Cold Spring Harbor Symp. Quant. Biol. 27, 1-24, 1962).

Binding Sites↗
PubMed1982

Molecular symmetry of the MoFe protein of nitrogenase. Structural homology/nitrogen fixation/x-ray crystallography.

X-ray diffraction data to 2.4-A resolution have been collected for native monoclinic crystals of the MoFe protein of nitrogenase from Clostridium pasteurianum. The MoFe protein is an alpha 2 beta 2 tetramer of 220,000 molecular weight with 1 molecule in the crystallographic asymmetric unit. A 6-A resolution rotation function shows the orientation of the crystallographic diad and pseudo mutually perpendicular diads representing 2-fold relationships between alpha and beta chains. Hence, at least at low resolution, there exists structural homology between these two polypeptide chains.

Clostridium↗