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3tt6
From Proteopedia
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==Structure of ClpP from Bacillus subtilis in compressed state== | ==Structure of ClpP from Bacillus subtilis in compressed state== | ||
| - | <StructureSection load='3tt6' size='340' side='right' caption='[[3tt6]], [[Resolution|resolution]] 2.59Å' scene=''> | + | <StructureSection load='3tt6' size='340' side='right'caption='[[3tt6]], [[Resolution|resolution]] 2.59Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3tt6]] is a 7 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3tt6]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TT6 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.592Å</td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tt6 OCA], [https://pdbe.org/3tt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tt6 RCSB], [https://www.ebi.ac.uk/pdbsum/3tt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tt6 ProSAT]</span></td></tr> | |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3tt6" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Clp protease 3D structures|Clp protease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Kim | + | [[Category: Kim MK]] |
| - | [[Category: Lee | + | [[Category: Lee B-G]] |
| - | [[Category: Song | + | [[Category: Song HK]] |
| - | + | ||
Current revision
Structure of ClpP from Bacillus subtilis in compressed state
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