3t5c

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{{STRUCTURE_3t5c| PDB=3t5c | SCENE= }}
 
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===Crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis in different space group C2===
 
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{{ABSTRACT_PUBMED_22206988}}
 
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==Function==
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==Crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis in different space group C2==
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[[http://www.uniprot.org/uniprot/FAC13_MYCTU FAC13_MYCTU]] Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Catalyzes the activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. It has preference for the fatty acid with long chain length in the following order: hexacosanoic acid (C26), tetracosanoic acid (C24) and palmitic acid (C16).<ref>PMID:15937179</ref> <ref>PMID:20027301</ref> <ref>PMID:22560731</ref>
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<StructureSection load='3t5c' size='340' side='right'caption='[[3t5c]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3t5c]] is a 2 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=3T5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T5C FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5c OCA], [https://pdbe.org/3t5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t5c RCSB], [https://www.ebi.ac.uk/pdbsum/3t5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t5c ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Activation of fatty acids as acyl-adenylates by fatty acyl-AMP ligases (FAALs) in Mycobacterium tuberculosis is a variant of a classical theme that involves formation of acyl-CoA (coenzyme A) by fatty acyl-CoA ligases (FACLs). Here, we show that FAALs and FACLs possess similar structural fold and substrate specificity determinants, and the key difference is the absence of a unique insertion sequence in FACL13 structure. A systematic analysis shows a conserved hydrophobic anchorage of the insertion motif across several FAALs. Strikingly, mutagenesis of two phenylalanine residues, which are part of the anchorage, to alanine converts FAAL32 to FACL32. This insertion-based in silico analysis suggests the presence of FAAL homologues in several other non-mycobacterial genomes including eukaryotes. The work presented here establishes an elegant mechanism wherein an insertion sequence drives the functional divergence of FAALs from canonical FACLs.
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==About this Structure==
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Molecular Basis of the Functional Divergence of Fatty Acyl-AMP Ligase Biosynthetic Enzymes of Mycobacterium tuberculosis.,Goyal A, Verma P, Anandhakrishnan M, Gokhale RS, Sankaranarayanan R J Mol Biol. 2011 Dec 21. PMID:22206988<ref>PMID:22206988</ref>
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[[3t5c]] is a 2 chain structure with sequence from [http://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=3T5C OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:022206988</ref><references group="xtra"/><references/>
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</div>
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[[Category: Mycobacterium tuberculosis h37rv]]
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<div class="pdbe-citations 3t5c" style="background-color:#fffaf0;"></div>
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[[Category: Goyal, A.]]
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== References ==
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[[Category: Sankaranarayanan, R.]]
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<references/>
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[[Category: Acetyl-coa synthetase like fold]]
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__TOC__
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[[Category: Amp-binding]]
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</StructureSection>
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[[Category: Ligase]]
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[[Category: Large Structures]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Goyal A]]
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[[Category: Sankaranarayanan R]]

Current revision

Crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis in different space group C2

PDB ID 3t5c

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