Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A.
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Animals↗
Biomedical subjects
D I Stuart
Publications and source records attributed to D I Stuart.
Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution.
The structure determination of pyruvate kinase shows that each subunit of the tetrameric molecule consists of three domains. The largest of these domains has a remarkable similarity to the structure of triosephosphate isomerase. Another domain shows similarities to many other nucleotide binding proteins. We discuss these similarities and their implications for current arguments on protein taxonomy and evolution.
Animals↗
Structure of cat muscle pyruvate kinase at 0.26 nm resolution.
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Adenosine Diphosphate↗
The crystal and molecular structure of an osmium bispyridine adduct of thymine.
The bispyridine osmium adduct of thymine has been crystallised and subjected to an X-ray diffraction analysis. It crystallises in the triclinic space group P1, with cell dimensions a equals 7.975(3), b equals 10.381(3), c equals 11.036(3) A, alpha equals 82.73(2)degrees, beta equals 77.22(3) degrees, gamma equals 101.75(3), and with two molecules in the unit cell. The analysis has shown that the osmium reagent has added cis across the 5,6 thymine bond.
Binding Sites↗
Alpha-lactalbumin possesses a novel calcium binding loop.
Calcium performs a unique role in biology, achieving biological effects through highly specific interactions with and modulation of target proteins. It has been proposed that calcium-modulated proteins possess a characteristic, evolutionarily related, binding fold, known as the EF-hand. The high-resolution X-ray structure of alpha-lactalbumin reveals a Ca2+ binding fold that resembles an EF-hand only superficially and presumably has no evolutionary relationship with it. However, there is clear homology with the corresponding loop in c-type lysozyme (the 'parent' molecule of alpha-lactalbumin). This study, at 1.7 A resolution, represents one of the most accurate analyses of a calcium binding protein yet reported.
Binding Sites↗