This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3wdb

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

N-terminal domain of Mycobacterium tuberculosis ClpC1

Structural highlights

3wdb is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.37Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Publication Abstract from PubMed

Cyclomarin A (CymA) was identified as a mycobactericidal compound targeting ClpC1. However, the target was identified based on pulldown experiments and in vitro binding data, without direct functional evidence in mycobacteria. Here we show that CymA specifically binds to the N-terminal domain of ClpC1. In addition we have determined the co-crystal structure of CymA bound to the N-terminal domain of ClpC1 to high resolution. Based on the structure of the complex several mutations were engineered into ClpC1, which showed reduced CymA binding in vitro. The ClpC1 mutants were overexpressed in mycobacteria and two showed resistance to CymA, providing the first direct evidence that ClpC1 is the target of CymA. Phe(80) is important in vitro and in cells for the ClpC1-CymA interaction and this explains why other bacteria are resistant to CymA. A model for how CymA binding to the N-terminal domain of ClpC1 leads to uncontrolled proteolysis by the associated ClpP protease machinery is discussed.

Structural basis of mycobacterial inhibition by cyclomarin A.,Vasudevan D, Rao SP, Noble CG J Biol Chem. 2013 Oct 25;288(43):30883-91. doi: 10.1074/jbc.M113.493767. Epub, 2013 Sep 10. PMID:24022489^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Vasudevan D, Rao SP, Noble CG. Structural basis of mycobacterial inhibition by cyclomarin A. J Biol Chem. 2013 Oct 25;288(43):30883-91. doi: 10.1074/jbc.M113.493767. Epub, 2013 Sep 10. PMID:24022489 doi:http://dx.doi.org/10.1074/jbc.M113.493767

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3wdb"

Categories: Large Structures | Mycobacterium tuberculosis | Noble CG | Vasudevan D

@@ Line 1: / Line 1: @@
 ==N-terminal domain of Mycobacterium tuberculosis ClpC1==
-<StructureSection load='3wdb' size='340' side='right' caption='[[3wdb]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
+<StructureSection load='3wdb' size='340' side='right'caption='[[3wdb]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3wdb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WDB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WDB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3wdb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WDB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 1.37&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wdc|3wdc]], [[3wdd|3wdd]], [[3wde|3wde]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpC ([http://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'>[https://proteopedia.org/fgij/fg.htm?mol=3wdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wdb OCA], [https://pdbe.org/3wdb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wdb RCSB], [https://www.ebi.ac.uk/pdbsum/3wdb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wdb ProSAT]</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=3wdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wdb OCA], [http://pdbe.org/3wdb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wdb RCSB], [http://www.ebi.ac.uk/pdbsum/3wdb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wdb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Noble, C G]]
+[[Category: Large Structures]]
-[[Category: Vasudevan, D]]
+[[Category: Mycobacterium tuberculosis]]
-[[Category: Chaperone]]
+[[Category: Noble CG]]
+[[Category: Vasudevan D]]

3wdb

From Proteopedia

Current revision

N-terminal domain of Mycobacterium tuberculosis ClpC1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox