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| | <StructureSection load='4ryf' size='340' side='right'caption='[[4ryf]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='4ryf' size='340' side='right'caption='[[4ryf]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ryf]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4RYF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ryf]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RYF FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fzs|2fzs]], [[4jcq|4jcq]], [[4jct|4jct]]</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=4ryf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryf OCA], [https://pdbe.org/4ryf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ryf RCSB], [https://www.ebi.ac.uk/pdbsum/4ryf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryf ProSAT]</span></td></tr> |
| - | <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=1639 "Bacterium monocytogenes hominis" Nyfeldt 1932])</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://proteopedia.org/fgij/fg.htm?mol=4ryf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryf OCA], [http://pdbe.org/4ryf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ryf RCSB], [http://www.ebi.ac.uk/pdbsum/4ryf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q8Y7Y1_LISMO Q8Y7Y1_LISMO]] 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).[HAMAP-Rule:MF_00444] [[http://www.uniprot.org/uniprot/CLPP_LISMO CLPP_LISMO]] 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). | + | [https://www.uniprot.org/uniprot/Q8Y7Y1_LISMO Q8Y7Y1_LISMO] 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).[HAMAP-Rule:MF_00444] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium monocytogenes hominis nyfeldt 1932]] | |
| - | [[Category: Endopeptidase Clp]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dahmen, M]] | + | [[Category: Listeria monocytogenes]] |
| - | [[Category: Groll, M]] | + | [[Category: Dahmen M]] |
| - | [[Category: Sieber, S A]] | + | [[Category: Groll M]] |
| - | [[Category: Vielberg, M T]]
| + | [[Category: Sieber SA]] |
| - | [[Category: Clpp]] | + | [[Category: Vielberg M-T]] |
| - | [[Category: Enzyme catalysis]] | + | |
| - | [[Category: Heterocomplex]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Pathogenic bacteria]]
| + | |
| - | [[Category: Proteolysis]]
| + | |
| - | [[Category: Ser-protease]]
| + | |
| Structural highlights
Function
Q8Y7Y1_LISMO 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).[HAMAP-Rule:MF_00444]
Publication Abstract from PubMed
Listeria monocytogenes is a devastating bacterial pathogen. Its virulence and intracellular stress tolerance are supported by caseinolytic protease P (ClpP), an enzyme that is conserved among bacteria. L. monocytogenes expresses two ClpP isoforms that are only distantly related by sequence and differ in catalysis, oligomerization, active-site composition, and N-terminal interaction sites for associated AAA(+) chaperones. The crystal structure of the ClpP1/2 heterocomplex from L. monocytogenes was solved, and in combination with biochemical studies, it provides insights into the mode of action. The results demonstrate that structural interlocking of LmClpP1 with LmClpP2 leads to the formation of a tetradecamer, aligns all 14 active sites, and enhances proteolytic activity. Furthermore, the catalytic center was identified as being responsible for the transient stability of ClpPs.
Structure and mechanism of the caseinolytic protease ClpP1/2 heterocomplex from Listeria monocytogenes.,Dahmen M, Vielberg MT, Groll M, Sieber SA Angew Chem Int Ed Engl. 2015 Mar 16;54(12):3598-602. doi: 10.1002/anie.201409325., Epub 2015 Jan 28. PMID:25630955[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dahmen M, Vielberg MT, Groll M, Sieber SA. Structure and mechanism of the caseinolytic protease ClpP1/2 heterocomplex from Listeria monocytogenes. Angew Chem Int Ed Engl. 2015 Mar 16;54(12):3598-602. doi: 10.1002/anie.201409325., Epub 2015 Jan 28. PMID:25630955 doi:http://dx.doi.org/10.1002/anie.201409325
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