1fro
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HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR
OverviewOverview
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.
About this StructureAbout this Structure
1FRO is a Single protein structure of sequence from Homo sapiens with ZN and GSB as ligands. Active as Lactoylglutathione lyase, with EC number 4.4.1.5 Structure known Active Sites: GH1, GH2, GH3, GH4, HD2, HD3, HD4, HD5, ZN1, ZN2, ZN3 and ZN4. 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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