1fro: Difference between revisions

Revision as of 03:50, 1 July 2008

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File:1fro.png

Template:STRUCTURE 1fro

HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITORHUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR

Template:ABSTRACT PUBMED 9218781

About this StructureAbout this Structure

1FRO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping., Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA, EMBO J. 1997 Jun 16;16(12):3386-95. PMID:9218781

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OCA

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-'''HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR'''
+===HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR===
-==Overview==
+<!--
-The zinc metalloenzyme glyoxalase I catalyses the glutathione-dependent inactivation of toxic methylglyoxal. The structure of the dimeric human enzyme in complex with S-benzyl-glutathione has been determined by multiple isomorphous replacement (MIR) and refined at 2.2 A resolution. Each monomer consists of two domains. Despite only low sequence homology between them, these domains are structurally equivalent and appear to have arisen by a gene duplication. On the other hand, there is no structural homology to the 'glutathione binding domain' found in other glutathione-linked proteins. 3D domain swapping of the N- and C-terminal domains has resulted in the active site being situated in the dimer interface, with the inhibitor and essential zinc ion interacting with side chains from both subunits. Two structurally equivalent residues from each domain contribute to a square pyramidal coordination of the zinc ion, rarely seen in zinc enzymes. Comparison of glyoxalase I with other known structures shows the enzyme to belong to a new structural family which includes the Fe2+-dependent dihydroxybiphenyl dioxygenase and the bleomycin resistance protein. This structural family appears to allow members to form with or without domain swapping.
+The line below this paragraph, {{ABSTRACT_PUBMED_9218781}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9218781 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9218781}}
 ==About this Structure==
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 [[Category: Glyoxalase i]]
 [[Category: Lactoylglutathione lyase]]
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