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| | <StructureSection load='5yx6' size='340' side='right'caption='[[5yx6]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5yx6' size='340' side='right'caption='[[5yx6]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yx6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YX6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yx6]] is a 4 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=5YX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YX6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv3272 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5yx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yx6 OCA], [https://pdbe.org/5yx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yx6 RCSB], [https://www.ebi.ac.uk/pdbsum/5yx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yx6 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=5yx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yx6 OCA], [https://pdbe.org/5yx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yx6 RCSB], [https://www.ebi.ac.uk/pdbsum/5yx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yx6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/COATR_MYCTU COATR_MYCTU] Probably involved in fatty acid metabolism. Binds to fatty acyl-CoAs of varying carbon chain lengths, with the highest binding affinity for palmitoyl-CoA (C16:0). In vitro, alters the cell wall lipid profile and protects mycobacteria from acidic, oxidative and antibiotic stress. May play a significant role in host-pathogen interaction.<ref>PMID:30342240</ref> |
| | <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: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Ansari, A]] | + | [[Category: Ansari A]] |
| - | [[Category: Pratap, J Venkatesh]]
| + | [[Category: Shrimant KS]] |
| - | [[Category: Shrimant, K S]] | + | [[Category: Venkatesh Pratap J]] |
| - | [[Category: Coa transferase]] | + | |
| - | [[Category: Fatty acid metabolism]]
| + | |
| - | [[Category: Rv3272]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Tuberculosis]]
| + | |
| Structural highlights
Function
COATR_MYCTU Probably involved in fatty acid metabolism. Binds to fatty acyl-CoAs of varying carbon chain lengths, with the highest binding affinity for palmitoyl-CoA (C16:0). In vitro, alters the cell wall lipid profile and protects mycobacteria from acidic, oxidative and antibiotic stress. May play a significant role in host-pathogen interaction.[1]
Publication Abstract from PubMed
The availability of complete genome sequence of Mycobacterium tuberculosis has provided an important tool to understand the mycobacterial biology with respect to host-pathogen interaction, which is an unmet need of the hour owing to continuous increasing drug resistance. Hypothetical proteins are often an overlooked pool though half the genome encodes for such proteins of unknown function that could potentially play vital roles in mycobacterial biology. In this context, we report the structural and functional characterization of the hypothetical protein Rv3272. Sequence analysis classifies Rv3272 as a Family III CoA transferase with the classical two domain structure and conserved Aspartate residue (D175). The crystal structure of the wild type protein (2.2A) demonstrated the associated inter-locked dimer while that of the D175A mutant co-crystallized with octanoyl-CoA demonstrated relative movement between the two domains. Isothermal titration calorimetry studies indicate that Rv3272 binds to fatty acyl-CoAs of varying carbon chain lengths, with palmitoyl-CoA (C16:0) exhibiting maximum affinity. To determine the functional relevance of Rv3272 in mycobacterial biology, we ectopically expressed Rv3272 in M. smegmatis and assessed that its expression encodes significant alteration in cell surface with marked differences in triacylglycerol accumulation. Additionally, Rv3272 expression protects mycobacteria from acidic, oxidative and antibiotic stress under in vitro conditions. Taken together, these studies indicate a significant role for Rv3272 in host-pathogen interaction.
Rv3272 encodes a novel Family III CoA transferase that alters the cell wall lipid profile and protects mycobacteria from acidic and oxidative stress.,Karade SS, Pandey S, Ansari A, Das S, Tripathi S, Arora A, Chopra S, Pratap JV, Dasgupta A Biochim Biophys Acta Proteins Proteom. 2018 Oct 17. pii: S1570-9639(18)30180-8., doi: 10.1016/j.bbapap.2018.10.011. PMID:30342240[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Karade SS, Pandey S, Ansari A, Das S, Tripathi S, Arora A, Chopra S, Pratap JV, Dasgupta A. Rv3272 encodes a novel Family III CoA transferase that alters the cell wall lipid profile and protects mycobacteria from acidic and oxidative stress. Biochim Biophys Acta Proteins Proteom. 2018 Oct 17. pii: S1570-9639(18)30180-8., doi: 10.1016/j.bbapap.2018.10.011. PMID:30342240 doi:http://dx.doi.org/10.1016/j.bbapap.2018.10.011
- ↑ Karade SS, Pandey S, Ansari A, Das S, Tripathi S, Arora A, Chopra S, Pratap JV, Dasgupta A. Rv3272 encodes a novel Family III CoA transferase that alters the cell wall lipid profile and protects mycobacteria from acidic and oxidative stress. Biochim Biophys Acta Proteins Proteom. 2018 Oct 17. pii: S1570-9639(18)30180-8., doi: 10.1016/j.bbapap.2018.10.011. PMID:30342240 doi:http://dx.doi.org/10.1016/j.bbapap.2018.10.011
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