1usp
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1usp |SIZE=350|CAPTION= <scene name='initialview01'>1usp</scene>, resolution 1.9Å | |PDB= 1usp |SIZE=350|CAPTION= <scene name='initialview01'>1usp</scene>, resolution 1.9Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1usp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1usp OCA], [http://www.ebi.ac.uk/pdbsum/1usp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1usp RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Mcsweeney, S.]] | [[Category: Mcsweeney, S.]] | ||
[[Category: Meunier-Jamin, C.]] | [[Category: Meunier-Jamin, C.]] | ||
| - | [[Category: GOL]] | ||
[[Category: 2-cys peroxidase]] | [[Category: 2-cys peroxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:39 2008'' |
Revision as of 21:14, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN FROM DEINOCOCCUS RADIODURANS
Overview
The three-dimensional structure of the organic hydroperoxide resistance protein (OHRP) from Deinococcus radiodurans as determined using single crystal xray diffraction techniques is reported. Comparison of the structure with that obtained for OHRP from Pseudomonas aeruginosa reveals that the polypeptide chain of OHRPs can adopt two significantly different conformations ("in" and "out") in the region of the active site disulfide moiety. It is postulated that the closed configuration is consistent with efficient catalysis of the reduction of organic hydroperoxides, whereas the open form is required for enzyme recycling. Comparison of the structures of OHRP and that of the osmotically induced protein C (OsmC) from Mycoplasma pneumoniae shows that OHRPs and OsmCs are structurally homologous, perhaps indicating related functions for the two families of proteins.
About this Structure
1USP is a Protein complex structure of sequences from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide?, Meunier-Jamin C, Kapp U, Leonard GA, McSweeney S, J Biol Chem. 2004 Jun 11;279(24):25830-7. Epub 2004 Mar 30. PMID:15054099
Page seeded by OCA on Mon Mar 31 00:14:39 2008
