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3ktg

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==Structure of ClpP from Bacillus subtilis in monoclinic crystal form==
==Structure of ClpP from Bacillus subtilis in monoclinic crystal form==
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<StructureSection load='3ktg' size='340' side='right' caption='[[3ktg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='3ktg' size='340' side='right'caption='[[3ktg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ktg]] 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=3KTG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KTG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ktg]] 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=3KTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KTG FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kth|3kth]], [[3kti|3kti]], [[3ktj|3ktj]], [[3ktk|3ktk]]</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;'>[[3kth|3kth]], [[3kti|3kti]], [[3ktj|3ktj]], [[3ktk|3ktk]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP, yvdN, BSU34540 ([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, yvdN, BSU34540 ([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=3ktg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ktg OCA], [http://pdbe.org/3ktg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ktg RCSB], [http://www.ebi.ac.uk/pdbsum/3ktg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ktg 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=3ktg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ktg OCA], [https://pdbe.org/3ktg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ktg RCSB], [https://www.ebi.ac.uk/pdbsum/3ktg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ktg 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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Clp Protease|Clp Protease]]
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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: Brotz-Oesterhelt, H]]
[[Category: Brotz-Oesterhelt, H]]
[[Category: Lee, B G]]
[[Category: Lee, B G]]

Revision as of 07:51, 10 November 2021

Structure of ClpP from Bacillus subtilis in monoclinic crystal form

PDB ID 3ktg

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