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| | <StructureSection load='4z0m' size='340' side='right'caption='[[4z0m]], [[Resolution|resolution]] 1.97Å' scene=''> | | <StructureSection load='4z0m' size='340' side='right'caption='[[4z0m]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4z0m]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z0M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z0M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4z0m]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z0M FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qka|3qka]]</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]] 1.97Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">echA5, Rv0675 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=4z0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z0m OCA], [https://pdbe.org/4z0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z0m RCSB], [https://www.ebi.ac.uk/pdbsum/4z0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z0m ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] </span></td></tr>
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| - | <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=4z0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z0m OCA], [http://pdbe.org/4z0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z0m RCSB], [http://www.ebi.ac.uk/pdbsum/4z0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z0m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/I6Y4E8_MYCTU I6Y4E8_MYCTU] |
| | <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: Enoyl-CoA hydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Chaudhary, S]] | + | [[Category: Chaudhary S]] |
| - | [[Category: Gokhale, R S]] | + | [[Category: Gokhale RS]] |
| - | [[Category: Beta oxidation]]
| + | |
| - | [[Category: Enoyl hydrase]]
| + | |
| - | [[Category: Enoyl-coa hydratase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Lyase]]
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| Structural highlights
Function
I6Y4E8_MYCTU
Publication Abstract from PubMed
Mycobacterium tuberculosis (Mtb) can survive in hypoxic necrotic tissue by assimilating energy from host-derived fatty acids. While the expanded repertoire of beta-oxidation auxiliary enzymes is considered crucial for Mtb adaptability, delineating their functional relevance has been challenging. Here, we show that the Mtb fatty acid degradation (FadAB) complex cannot selectively break down cis fatty acyl substrates. We demonstrate that the stereoselective binding of fatty acyl substrates in the Mtb FadB pocket is due to the steric hindrance from Phe287 residue. By developing a functional screen, we classify the family of Mtb Ech proteins as monofunctional or bifunctional enzymes, three of which complement the FadAB complex to degrade cis fatty acids. Crystal structure determination of two cis-trans enoyl coenzyme A (CoA) isomerases reveals distinct placement of active-site residue in Ech enzymes. Our studies thus reveal versatility of Mtb lipid-remodeling enzymes and identify an essential role of stand-alone cis-trans enoyl CoA isomerases in mycobacterial biology.
Unsaturated Lipid Assimilation by Mycobacteria Requires Auxiliary cis-trans Enoyl CoA Isomerase.,Srivastava S, Chaudhary S, Thukral L, Shi C, Gupta RD, Gupta R, Priyadarshan K, Vats A, Haque AS, Sankaranarayanan R, Natarajan VT, Sharma R, Aldrich CC, Gokhale RS Chem Biol. 2015 Dec 17;22(12):1577-87. doi: 10.1016/j.chembiol.2015.10.009. Epub , 2015 Nov 25. PMID:26628360[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Srivastava S, Chaudhary S, Thukral L, Shi C, Gupta RD, Gupta R, Priyadarshan K, Vats A, Haque AS, Sankaranarayanan R, Natarajan VT, Sharma R, Aldrich CC, Gokhale RS. Unsaturated Lipid Assimilation by Mycobacteria Requires Auxiliary cis-trans Enoyl CoA Isomerase. Chem Biol. 2015 Dec 17;22(12):1577-87. doi: 10.1016/j.chembiol.2015.10.009. Epub , 2015 Nov 25. PMID:26628360 doi:http://dx.doi.org/10.1016/j.chembiol.2015.10.009
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