4u0g
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| + | {{Large structure}} | ||
==Crystal Structure of M. tuberculosis ClpP1P2 bound to ADEP and agonist== | ==Crystal Structure of M. tuberculosis ClpP1P2 bound to ADEP and agonist== | ||
<StructureSection load='4u0g' size='340' side='right' caption='[[4u0g]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='4u0g' size='340' side='right' caption='[[4u0g]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| Line 6: | Line 7: | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=39Y:(2E,5S)-5-METHYLHEPT-2-ENOIC+ACID'>39Y</scene>, <scene name='pdbligand=3A0:(2S,4S)-4-METHYLPIPERIDINE-2-CARBOXYLIC+ACID'>3A0</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=WFP:3,5-DIFLUORO-L-PHENYLALANINE'>WFP</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=39Y:(2E,5S)-5-METHYLHEPT-2-ENOIC+ACID'>39Y</scene>, <scene name='pdbligand=3A0:(2S,4S)-4-METHYLPIPERIDINE-2-CARBOXYLIC+ACID'>3A0</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=WFP:3,5-DIFLUORO-L-PHENYLALANINE'>WFP</scene></td></tr> | ||
<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> | <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> | ||
| - | <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=4u0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u0g RCSB], [http://www.ebi.ac.uk/pdbsum/4u0g 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=4u0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0g OCA], [http://pdbe.org/4u0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u0g RCSB], [http://www.ebi.ac.uk/pdbsum/4u0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u0g ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | {{Large structure}} | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CLPP2_MYCTU CLPP2_MYCTU]] 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). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA.[HAMAP-Rule:MF_00444]<ref>PMID:20025669</ref> <ref>PMID:23314154</ref> [[http://www.uniprot.org/uniprot/CLPP1_MYCTU CLPP1_MYCTU]] 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). | [[http://www.uniprot.org/uniprot/CLPP2_MYCTU CLPP2_MYCTU]] 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). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA.[HAMAP-Rule:MF_00444]<ref>PMID:20025669</ref> <ref>PMID:23314154</ref> [[http://www.uniprot.org/uniprot/CLPP1_MYCTU CLPP1_MYCTU]] 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). | ||
| Line 18: | Line 20: | ||
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 4u0g" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Clp Protease|Clp Protease]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:33, 5 August 2016
Warning: this is a large structure, and loading might take a long time or not happen at all.
Crystal Structure of M. tuberculosis ClpP1P2 bound to ADEP and agonist
| |||||||||||
