3tt7: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:3tt7.png|left|200px]]
{{STRUCTURE_3tt7|  PDB=3tt7  |  SCENE=  }}  
{{STRUCTURE_3tt7|  PDB=3tt7  |  SCENE=  }}  
===Structure of ClpP from Bacillus subtilis in complex with DFP===
===Structure of ClpP from Bacillus subtilis in complex with DFP===
{{ABSTRACT_PUBMED_22080375}}


{{ABSTRACT_PUBMED_22080375}}
==Function==
[[http://www.uniprot.org/uniprot/CLPP_BACSU CLPP_BACSU]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor.<ref>PMID:16899079</ref> 


==About this Structure==
==About this Structure==
[[3tt7]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TT7 OCA].  
[[3tt7]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TT7 OCA].  


==See Also==
==Reference==
*[[Clp Protease|Clp Protease]]
<ref group="xtra">PMID:022080375</ref><references group="xtra"/><references/>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Endopeptidase Clp]]
[[Category: Endopeptidase Clp]]

Revision as of 10:33, 30 June 2013

Template:STRUCTURE 3tt7

Structure of ClpP from Bacillus subtilis in complex with DFPStructure of ClpP from Bacillus subtilis in complex with DFP

Template:ABSTRACT PUBMED 22080375

FunctionFunction

[CLPP_BACSU] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor.[1]

About this StructureAbout this Structure

3tt7 is a 7 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Lee BG, Kim MK, Song HK. Structural insights into the conformational diversity of ClpP from Bacillus subtilis. Mol Cells. 2011 Nov 9. PMID:22080375 doi:10.1007/s10059-011-0197-1
  1. Zellmeier S, Schumann W, Wiegert T. Involvement of Clp protease activity in modulating the Bacillus subtilissigmaw stress response. Mol Microbiol. 2006 Sep;61(6):1569-82. Epub 2006 Aug 8. PMID:16899079 doi:MMI5323

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA