3wdd: Difference between revisions
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==Mutant N-terminal domain of Mycobacterium tuberculosis ClpC1, F2Y, bound to Cyclomarin A== | ==Mutant N-terminal domain of Mycobacterium tuberculosis ClpC1, F2Y, bound to Cyclomarin A== | ||
<StructureSection load='3wdd' size='340' side='right' caption='[[3wdd]], [[Resolution|resolution]] 1.18Å' scene=''> | <StructureSection load='3wdd' size='340' side='right'caption='[[3wdd]], [[Resolution|resolution]] 1.18Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wdd]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3wdd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884] and [https://en.wikipedia.org/wiki/Streptomyces Streptomyces]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WDD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=WLU:(4R)-5-HYDROXY-N-METHYL-L-LEUCINE'>WLU</scene>, <scene name='pdbligand=WPA:(BETAR)-BETA-METHOXY-L-PHENYLALANINE'>WPA</scene>, <scene name='pdbligand=WRP:(BETAR)-BETA-HYDROXY-1-[(3R)-3-HYDROXY-2-METHYLBUTAN-2-YL]-L-TRYPTOPHAN'>WRP</scene>, <scene name='pdbligand=WVL:(2S,3R)-2-AMINO-3,5-DIMETHYLHEX-4-ENOIC+ACID'>WVL</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=WLU:(4R)-5-HYDROXY-N-METHYL-L-LEUCINE'>WLU</scene>, <scene name='pdbligand=WPA:(BETAR)-BETA-METHOXY-L-PHENYLALANINE'>WPA</scene>, <scene name='pdbligand=WRP:(BETAR)-BETA-HYDROXY-1-[(3R)-3-HYDROXY-2-METHYLBUTAN-2-YL]-L-TRYPTOPHAN'>WRP</scene>, <scene name='pdbligand=WVL:(2S,3R)-2-AMINO-3,5-DIMETHYLHEX-4-ENOIC+ACID'>WVL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wdb|3wdb]], [[3wdc|3wdc]], [[3wde|3wde]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wdb|3wdb]], [[3wdc|3wdc]], [[3wde|3wde]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpC ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wdd OCA], [https://pdbe.org/3wdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wdd RCSB], [https://www.ebi.ac.uk/pdbsum/3wdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wdd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CLPC1_MYCTU CLPC1_MYCTU]] ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | ||
<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: | [[Category: Large Structures]] | ||
[[Category: Streptomyces]] | |||
[[Category: Noble, C G]] | [[Category: Noble, C G]] | ||
[[Category: Vasudevan, D]] | [[Category: Vasudevan, D]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Chaperone-antimicrobial protein complex]] | [[Category: Chaperone-antimicrobial protein complex]] | ||
