1usp
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1usp.jpg|left|200px]]<br /><applet load="1usp" size=" | + | [[Image:1usp.jpg|left|200px]]<br /><applet load="1usp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1usp, resolution 1.9Å" /> | caption="1usp, resolution 1.9Å" /> | ||
'''ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN FROM DEINOCOCCUS RADIODURANS'''<br /> | '''ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN FROM DEINOCOCCUS RADIODURANS'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1USP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1USP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USP OCA]. |
==Reference== | ==Reference== | ||
| Line 20: | Line 20: | ||
[[Category: 2-cys peroxidase]] | [[Category: 2-cys peroxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:04:29 2008'' |
Revision as of 08:04, 3 February 2008
|
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 with as ligand. Known structural/functional Site: . 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 Sun Feb 3 10:04:29 2008
