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==Structure of ClpP from Escherichia coli in complex with ADEP1==
==Structure of ClpP from Escherichia coli in complex with ADEP1==
<StructureSection load='3mt6' size='340' side='right' caption='[[3mt6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3mt6' size='340' side='right'caption='[[3mt6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3mt6]] is a 56 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12] and [http://en.wikipedia.org/wiki/Streptomyces_hawaiiensis Streptomyces hawaiiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MT6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3mt6]] is a 56 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Streptomyces_hawaiiensis Streptomyces hawaiiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MT6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.901&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAA:N-METHYL-L-ALANINE'>MAA</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=OTT:(2E,4E,6E)-OCTA-2,4,6-TRIENOIC+ACID'>OTT</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAA:N-METHYL-L-ALANINE'>MAA</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=OTT:(2E,4E,6E)-OCTA-2,4,6-TRIENOIC+ACID'>OTT</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yg6|1yg6]], [[3ktg|3ktg]], [[3kth|3kth]], [[3kti|3kti]], [[3ktj|3ktj]], [[3ktk|3ktk]], [[1tyf|1tyf]], [[2fzs|2fzs]], [[1y7o|1y7o]]</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=3mt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mt6 OCA], [https://pdbe.org/3mt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mt6 RCSB], [https://www.ebi.ac.uk/pdbsum/3mt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mt6 ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=3mt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mt6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mt6 RCSB], [http://www.ebi.ac.uk/pdbsum/3mt6 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI] 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== 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>
</div>
</div>
<div class="pdbe-citations 3mt6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Clp Protease|Clp Protease]]
*[[Clp protease 3D structures|Clp protease 3D structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Endopeptidase Clp]]
[[Category: Escherichia coli K-12]]
[[Category: Escherichia coli k-12]]
[[Category: Large Structures]]
[[Category: Streptomyces hawaiiensis]]
[[Category: Streptomyces hawaiiensis]]
[[Category: Chung, Y S]]
[[Category: Chung YS]]
[[Category: Acypdepsipeptide antibiotic]]
[[Category: Caseinolytic protease]]
[[Category: Endopeptidase clp]]
[[Category: Hydrolase-antibiotic complex]]
[[Category: Protease ti]]
Retrieved from "https://proteopedia.org/3mt6"