1fro
From Proteopedia
(Difference between revisions)
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|PDB= 1fro |SIZE=350|CAPTION= <scene name='initialview01'>1fro</scene>, resolution 2.2Å | |PDB= 1fro |SIZE=350|CAPTION= <scene name='initialview01'>1fro</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=GH1:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH1</scene>, <scene name='pdbsite=GH2:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH2</scene>, <scene name='pdbsite=GH3:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH3</scene>, <scene name='pdbsite=GH4:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH4</scene>, <scene name='pdbsite=HD2:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD2</scene>, <scene name='pdbsite=HD3:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD3</scene>, <scene name='pdbsite=HD4:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD4</scene>, <scene name='pdbsite=HD5:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD5</scene>, <scene name='pdbsite=ZN1:Zn+Binding+Site+At+Dimer+Interface'>ZN1</scene>, <scene name='pdbsite=ZN2:Zn+Binding+Site+At+Dimer+Interface'>ZN2</scene>, <scene name='pdbsite=ZN3:Zn+Binding+Site+At+Dimer+Interface'>ZN3</scene> and <scene name='pdbsite=ZN4:Zn+Binding+Site+At+Dimer+Interface'>ZN4</scene> | |SITE= <scene name='pdbsite=GH1:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH1</scene>, <scene name='pdbsite=GH2:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH2</scene>, <scene name='pdbsite=GH3:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH3</scene>, <scene name='pdbsite=GH4:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH4</scene>, <scene name='pdbsite=HD2:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD2</scene>, <scene name='pdbsite=HD3:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD3</scene>, <scene name='pdbsite=HD4:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD4</scene>, <scene name='pdbsite=HD5:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD5</scene>, <scene name='pdbsite=ZN1:Zn+Binding+Site+At+Dimer+Interface'>ZN1</scene>, <scene name='pdbsite=ZN2:Zn+Binding+Site+At+Dimer+Interface'>ZN2</scene>, <scene name='pdbsite=ZN3:Zn+Binding+Site+At+Dimer+Interface'>ZN3</scene> and <scene name='pdbsite=ZN4:Zn+Binding+Site+At+Dimer+Interface'>ZN4</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GSB:S-BENZYL-GLUTATHIONE'>GSB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fro OCA], [http://www.ebi.ac.uk/pdbsum/1fro PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fro RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Autism, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138750 138750]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Cameron, A D.]] | [[Category: Cameron, A D.]] | ||
[[Category: Jones, T A.]] | [[Category: Jones, T A.]] | ||
| - | [[Category: GSB]] | ||
| - | [[Category: ZN]] | ||
[[Category: glyoxalase i]] | [[Category: glyoxalase i]] | ||
[[Category: lactoylglutathione lyase]] | [[Category: lactoylglutathione lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:28:59 2008'' |
Revision as of 17:29, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , and | ||||||
| Ligands: | , | ||||||
| Activity: | Lactoylglutathione lyase, with EC number 4.4.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1FRO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 20:28:59 2008
