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| | <StructureSection load='5e0n' size='340' side='right'caption='[[5e0n]], [[Resolution|resolution]] 2.06Å' scene=''> | | <StructureSection load='5e0n' size='340' side='right'caption='[[5e0n]], [[Resolution|resolution]] 2.06Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5e0n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E0N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E0N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5e0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E0N FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_3139 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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]] 2.061Å</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=5e0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e0n OCA], [http://pdbe.org/5e0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e0n RCSB], [http://www.ebi.ac.uk/pdbsum/5e0n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e0n ProSAT]</span></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=5e0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e0n OCA], [https://pdbe.org/5e0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e0n RCSB], [https://www.ebi.ac.uk/pdbsum/5e0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e0n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0QX16_MYCS2 A0QX16_MYCS2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mycs2]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Anandakrishnan, M]] | + | [[Category: Anandakrishnan M]] |
| - | [[Category: Haque, A S]] | + | [[Category: Haque AS]] |
| - | [[Category: Priyadarshan, K]] | + | [[Category: Priyadarshan K]] |
| - | [[Category: Sankaranarayanan, R]] | + | [[Category: Sankaranarayanan R]] |
| - | [[Category: Crotonase superfamily]]
| + | |
| - | [[Category: Fatty acid oxidation]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
A0QX16_MYCS2
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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