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2qmc
From Proteopedia
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[[Image:2qmc.png|left|200px]] | [[Image:2qmc.png|left|200px]] | ||
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{{STRUCTURE_2qmc| PDB=2qmc | SCENE= }} | {{STRUCTURE_2qmc| PDB=2qmc | SCENE= }} | ||
===Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant=== | ===Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant=== | ||
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==Reference== | ==Reference== | ||
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[[Category: Gamma-glutamyltransferase]] | [[Category: Gamma-glutamyltransferase]] | ||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
Revision as of 13:05, 30 January 2013
Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant
Template:ABSTRACT PUBMED 17960917
About this Structure
2qmc is a 4 chain structure with sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
Reference
- Morrow AL, Williams K, Sand A, Boanca G, Barycki JJ. Characterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis. Biochemistry. 2007 Nov 20;46(46):13407-14. Epub 2007 Oct 26. PMID:17960917 doi:10.1021/bi701599e
- Boanca G, Sand A, Okada T, Suzuki H, Kumagai H, Fukuyama K, Barycki JJ. Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad. J Biol Chem. 2007 Jan 5;282(1):534-41. Epub 2006 Nov 15. PMID:17107958 doi:10.1074/jbc.M607694200
