4mql
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of Antigen 85C-C209S mutant== | |
+ | <StructureSection load='4mql' size='340' side='right'caption='[[4mql]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4mql]] is a 1 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=4MQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MQL FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</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=4mql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mql OCA], [https://pdbe.org/4mql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mql RCSB], [https://www.ebi.ac.uk/pdbsum/4mql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mql ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A85C_MYCTU A85C_MYCTU] The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria to 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.<ref>PMID:1830294</ref> <ref>PMID:9162010</ref> | ||
- | + | ==See Also== | |
- | + | *[[Antigen 85 3D structures|Antigen 85 3D structures]] | |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Mycobacterium tuberculosis]] | ||
+ | [[Category: Boucau J]] | ||
+ | [[Category: Favrot L]] | ||
+ | [[Category: Grzegorzewicz AE]] | ||
+ | [[Category: Isailovic D]] | ||
+ | [[Category: Jackson M]] | ||
+ | [[Category: Lajiness DH]] | ||
+ | [[Category: Marvin RK]] | ||
+ | [[Category: Ronning DR]] |
Current revision
Crystal structure of Antigen 85C-C209S mutant
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