1qh3
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1qh3.jpg|left|200px]] | [[Image:1qh3.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1qh3", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1qh3| PDB=1qh3 | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE''' | '''HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE''' | ||
Line 30: | Line 27: | ||
[[Category: Olin, B.]] | [[Category: Olin, B.]] | ||
[[Category: Ridderstrom, M.]] | [[Category: Ridderstrom, M.]] | ||
- | [[Category: | + | [[Category: Metallo-hydrolase]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:15:46 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 03:15, 3 May 2008
HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE
Overview
BACKGROUND: Glyoxalase II, the second of two enzymes in the glyoxalase system, is a thiolesterase that catalyses the hydrolysis of S-D-lactoylglutathione to form glutathione and D-lactic acid. RESULTS: The structure of human glyoxalase II was solved initially by single isomorphous replacement with anomalous scattering and refined at a resolution of 1.9 A. The enzyme consists of two domains. The first domain folds into a four-layered beta sandwich, similar to that seen in the metallo-beta-lactamases. The second domain is predominantly alpha-helical. The active site contains a binuclear zinc-binding site and a substrate-binding site extending over the domain interface. The model contains acetate and cacodylate in the active site. A second complex was derived from crystals soaked in a solution containing the slow substrate, S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione. This complex was refined at a resolution of 1.45 A. It contains the added ligand in one molecule of the asymmetric unit and glutathione in the other. CONCLUSIONS: The arrangement of ligands around the zinc ions includes a water molecule, presumably in the form of a hydroxide ion, coordinated to both metal ions. This hydroxide ion is situated 2.9 A from the carbonyl carbon of the substrate in such a position that it could act as the nucleophile during catalysis. The reaction mechanism may also have implications for the action of metallo-beta-lactamases.
About this Structure
1QH3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue., Cameron AD, Ridderstrom M, Olin B, Mannervik B, Structure. 1999 Sep 15;7(9):1067-78. PMID:10508780 Page seeded by OCA on Sat May 3 06:15:46 2008