1sfr: Difference between revisions

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<StructureSection load='1sfr' size='340' side='right'caption='[[1sfr]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='1sfr' size='340' side='right'caption='[[1sfr]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1sfr]] is a 3 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=1SFR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SFR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1sfr]] is a 3 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=1SFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SFR FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dqy|1dqy]], [[1dqz|1dqz]], [[1f0p|1f0p]], [[1f0n|1f0n]], [[1va5|1va5]]</div></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]] 2.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fbpA ([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=1sfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sfr OCA], [https://pdbe.org/1sfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sfr RCSB], [https://www.ebi.ac.uk/pdbsum/1sfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sfr ProSAT], [https://www.topsan.org/Proteins/TBSGC/1sfr TOPSAN]</span></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=1sfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sfr OCA], [http://pdbe.org/1sfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sfr RCSB], [http://www.ebi.ac.uk/pdbsum/1sfr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sfr ProSAT], [http://www.topsan.org/Proteins/TBSGC/1sfr TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A85A_MYCTU A85A_MYCTU]] The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan, and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA.<ref>PMID:3141278</ref> <ref>PMID:12010501</ref> <ref>PMID:9162010</ref> <ref>PMID:21819455</ref>
[https://www.uniprot.org/uniprot/A85A_MYCTU A85A_MYCTU] The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan, and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA.<ref>PMID:3141278</ref> <ref>PMID:12010501</ref> <ref>PMID:9162010</ref> <ref>PMID:21819455</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Belisle, J T]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Besra, G S]]
[[Category: Belisle JT]]
[[Category: Ronning, D R]]
[[Category: Besra GS]]
[[Category: Sacchettini, J C]]
[[Category: Ronning DR]]
[[Category: Structural genomic]]
[[Category: Sacchettini JC]]
[[Category: Vissa, V]]
[[Category: Vissa V]]
[[Category: Alpha/beta hydrolase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Tbsgc]]
[[Category: Transferase]]
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