3pgm: Difference between revisions

[[Image:3pgm.gif|left|200px]]<br />

<applet load="3pgm" size="450" color="white" frame="true" align="right" spinBox="true"  

The structure of yeast phosphoglycerate mutase determined by X-ray, crystallographic and amino acid sequence studies has been interpreted in, terms of the chemical, kinetic and mechanistic observations made on this, enzyme. There are two histidine residues at the active site, with, imidazole groups almost parallel to each other and approximately 0.4 nm, apart, positioned close to the 2 and 3 positions of the substrate. The, simplest interpretation of the available information suggests that a, ping-pong type mechanism operates in which at least one of these histidine, residues participates in the phosphoryl transfer reaction. The flexible, C-terminal region also plays an important role in the enzymic reaction.

3PGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1PGM. The following page contains interesting information on the relation of 3PGM with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3PGM OCA].  

[[Category: Campbell, J.W.]]

[[Category: Hodgson, G.I.]]

[[Category: Watson, H.C.]]

[[Category: Winn, S.I.]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:10:35 2007''