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==Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis==
==Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis==
<StructureSection load='3p2l' size='340' side='right' caption='[[3p2l]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
<StructureSection load='3p2l' size='340' side='right'caption='[[3p2l]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3p2l]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Fratt Fratt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P2L FirstGlance]. <br>
<table><tr><td colspan='2'>[[3p2l]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Fratt Fratt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P2L FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP, FTT_0624 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=177416 FRATT])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP, FTT_0624 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=177416 FRATT])</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'>[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>
<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=3p2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p2l OCA], [http://pdbe.org/3p2l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3p2l RCSB], [http://www.ebi.ac.uk/pdbsum/3p2l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3p2l ProSAT]</span></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=3p2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p2l OCA], [https://pdbe.org/3p2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p2l RCSB], [https://www.ebi.ac.uk/pdbsum/3p2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p2l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CLPP_FRATT CLPP_FRATT]] 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.[HAMAP-Rule:MF_00444]  
[[https://www.uniprot.org/uniprot/CLPP_FRATT CLPP_FRATT]] 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.[HAMAP-Rule:MF_00444]  


==See Also==
==See Also==
*[[Clp Protease|Clp Protease]]
*[[Clp protease 3D structures|Clp protease 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Endopeptidase Clp]]
[[Category: Endopeptidase Clp]]
[[Category: Fratt]]
[[Category: Fratt]]
[[Category: Large Structures]]
[[Category: Anderson, W F]]
[[Category: Anderson, W F]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]

Revision as of 11:12, 18 May 2022

Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis

3p2l, resolution 2.29Å

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