1fro: Difference between revisions

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[[Image:1fro.gif|left|200px]]
[[Image:1fro.gif|left|200px]]


{{Structure
<!--
|PDB= 1fro |SIZE=350|CAPTION= <scene name='initialview01'>1fro</scene>, resolution 2.2&Aring;
The line below this paragraph, containing "STRUCTURE_1fro", creates the "Structure Box" on the page.
|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>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=GSB:S-BENZYL-GLUTATHIONE'>GSB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1fro| PDB=1fro  | SCENE= }}  
|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>
}}


'''HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR'''
'''HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR'''
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[[Category: Cameron, A D.]]
[[Category: Cameron, A D.]]
[[Category: Jones, T A.]]
[[Category: Jones, T A.]]
[[Category: glyoxalase i]]
[[Category: Glyoxalase i]]
[[Category: lactoylglutathione lyase]]
[[Category: Lactoylglutathione lyase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:41:17 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:28:59 2008''

Revision as of 16:41, 2 May 2008

File:1fro.gif

Template:STRUCTURE 1fro

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. 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 Page seeded by OCA on Fri May 2 16:41:17 2008

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