4ubu
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Structure of a modified C93S variant of the 3-ketoacyl-CoA thiolase FadA5 from M. tuberculosis in complex with CoA== |
| + | <StructureSection load='4ubu' size='340' side='right' caption='[[4ubu]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ubu]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UBU FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OAS:O-ACETYLSERINE'>OAS</scene></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=4ubu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ubu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ubu RCSB], [http://www.ebi.ac.uk/pdbsum/4ubu PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | With the exception of HIV, tuberculosis (TB) is the leading cause of mortality among infectious diseases. The urgent need to develop new antitubercular drugs is apparent due to the increasing number of drug-resistant Mycobacterium tuberculosis (Mtb) strains. Proteins involved in cholesterol import and metabolism have recently been discovered as potent targets against TB. FadA5, a thiolase from Mtb, is catalyzing the last step of the beta-oxidation reaction of the cholesterol side-chain degradation under release of critical metabolites and was shown to be of importance during the chronic stage of TB infections. To gain structural and mechanistic insight on FadA5, we characterized the enzyme in different stages of the cleavage reaction and with a steroid bound to the binding pocket. Structural comparisons to human thiolases revealed that it should be possible to target FadA5 specifically, and the steroid-bound structure provides a solid basis for the development of inhibitors against FadA5. | ||
| - | + | FadA5 a Thiolase from Mycobacterium tuberculosis: A Steroid-Binding Pocket Reveals the Potential for Drug Development against Tuberculosis.,Schaefer CM, Lu R, Nesbitt NM, Schiebel J, Sampson NS, Kisker C Structure. 2014 Dec 3. pii: S0969-2126(14)00355-4. doi:, 10.1016/j.str.2014.10.010. PMID:25482540<ref>PMID:25482540</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kisker, C]] | ||
| + | [[Category: Schaefer, C M]] | ||
| + | [[Category: Acetylated]] | ||
| + | [[Category: Degradative thiolase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 12:41, 17 December 2014
Structure of a modified C93S variant of the 3-ketoacyl-CoA thiolase FadA5 from M. tuberculosis in complex with CoA
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