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3tt6

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==Structure of ClpP from Bacillus subtilis in compressed state==
==Structure of ClpP from Bacillus subtilis in compressed state==
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<StructureSection load='3tt6' size='340' side='right' caption='[[3tt6]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
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<StructureSection load='3tt6' size='340' side='right'caption='[[3tt6]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tt6]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TT6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tt6]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. 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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tt7|3tt7]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tt7|3tt7]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr>
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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://pdbe.org/3tt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tt6 RCSB], [http://www.ebi.ac.uk/pdbsum/3tt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tt6 ProSAT]</span></td></tr>
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<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>
</table>
</table>
== Function ==
== 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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[[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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</div>
</div>
<div class="pdbe-citations 3tt6" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3tt6" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Clp protease 3D structures|Clp protease 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Vibrio subtilis ehrenberg 1835]]
[[Category: Vibrio subtilis ehrenberg 1835]]
[[Category: Endopeptidase Clp]]
[[Category: Endopeptidase Clp]]
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[[Category: Large Structures]]
[[Category: Kim, M K]]
[[Category: Kim, M K]]
[[Category: Lee, B G]]
[[Category: Lee, B G]]
[[Category: Song, H K]]
[[Category: Song, H K]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]

Revision as of 05:44, 13 July 2022

Structure of ClpP from Bacillus subtilis in compressed state

PDB ID 3tt6

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