1qh3
From Proteopedia
(New page: 200px<br /> <applet load="1qh3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qh3, resolution 1.9Å" /> '''HUMAN GLYOXALASE II ...) |
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caption="1qh3, resolution 1.9Å" /> | caption="1qh3, resolution 1.9Å" /> | ||
'''HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE'''<br /> | '''HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QH3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, CAC, ACT, MN and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydroxyacylglutathione_hydrolase Hydroxyacylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6] Full crystallographic information is available from [http:// | + | 1QH3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CAC:'>CAC</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydroxyacylglutathione_hydrolase Hydroxyacylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QH3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: metallo-hydrolase]] | [[Category: metallo-hydrolase]] | ||
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Revision as of 14:44, 15 February 2008
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HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE
Contents |
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.
Disease
Known diseases associated with this structure: Glyoxalase II deficiency OMIM:[138760]
About this Structure
1QH3 is a Single protein structure of sequence from Homo sapiens with , , , and as ligands. Active as Hydroxyacylglutathione hydrolase, with EC number 3.1.2.6 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 Fri Feb 15 16:44:36 2008
Categories: Homo sapiens | Hydroxyacylglutathione hydrolase | Single protein | Cameron, A.D. | Mannervik, B. | Olin, B. | Ridderstrom, M. | ACT | CAC | CL | MN | ZN | Metallo-hydrolase
