3tt6

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tt6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tt6 RCSB], [http://www.ebi.ac.uk/pdbsum/3tt6 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tt6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tt6 RCSB], [http://www.ebi.ac.uk/pdbsum/3tt6 PDBsum]</span></td></tr>
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== Function ==
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[[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>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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*[[Clp Protease|Clp Protease]]
== References ==
== References ==
<references/>
<references/>

Revision as of 12:42, 25 December 2014

Structure of ClpP from Bacillus subtilis in compressed state

3tt6, resolution 2.59Å

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