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3t5c

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Revision as of 13:37, 24 December 2014

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

Structural highlights

3t5c is a 2 chain structure with sequence from Mycobacterium tuberculosis h37rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3t5a, 3t5b
Gene:	fadD13, MT3174, Rv3089 (Mycobacterium tuberculosis H37Rv)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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).^[1] ^[2] ^[3]

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Singh A, Gupta R, Vishwakarma RA, Narayanan PR, Paramasivan CN, Ramanathan VD, Tyagi AK. Requirement of the mymA operon for appropriate cell wall ultrastructure and persistence of Mycobacterium tuberculosis in the spleens of guinea pigs. J Bacteriol. 2005 Jun;187(12):4173-86. PMID:15937179 doi:10.1128/JB.187.12.4173-4186.2005
↑ Khare G, Gupta V, Gupta RK, Gupta R, Bhat R, Tyagi AK. Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA Synthetase (FadD13) of Mycobacterium tuberculosis. PLoS One. 2009 Dec 21;4(12):e8387. doi: 10.1371/journal.pone.0008387. PMID:20027301 doi:10.1371/journal.pone.0008387
↑ Andersson CS, Lundgren CA, Magnusdottir A, Ge C, Wieslander A, Molina DM, Hogbom M. The Mycobacterium tuberculosis Very-Long-Chain Fatty Acyl-CoA Synthetase: Structural Basis for Housing Lipid Substrates Longer than the Enzyme. Structure. 2012 May 2. PMID:22560731 doi:10.1016/j.str.2012.03.012
↑ Goyal A, Verma P, Anandhakrishnan M, Gokhale RS, Sankaranarayanan R. Molecular Basis of the Functional Divergence of Fatty Acyl-AMP Ligase Biosynthetic Enzymes of Mycobacterium tuberculosis. J Mol Biol. 2011 Dec 21. PMID:22206988 doi:10.1016/j.jmb.2011.12.031

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3t5c"

@@ Line 7: / Line 7: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t5c RCSB], [http://www.ebi.ac.uk/pdbsum/3t5c PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3t5c

From Proteopedia

Revision as of 13:37, 24 December 2014

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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