3t5a: Difference between revisions
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==Crystal structure of N-terminal domain of FAAL28 G330W mutant from Mycobacterium tuberculosis== | |||
<StructureSection load='3t5a' size='340' side='right' caption='[[3t5a]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3t5a]] is a 1 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=3T5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T5A FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e53|3e53]], [[3t5b|3t5b]], [[3t5c|3t5c]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acoas, fadD28, MT3011, Rv2941 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 Mycobacterium tuberculosis H37Rv])</td></tr> | |||
<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=3t5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t5a RCSB], [http://www.ebi.ac.uk/pdbsum/3t5a PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:22206988</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mycobacterium tuberculosis h37rv]] | [[Category: Mycobacterium tuberculosis h37rv]] | ||
[[Category: Goyal, A | [[Category: Goyal, A]] | ||
[[Category: Sankaranarayanan, R | [[Category: Sankaranarayanan, R]] | ||
[[Category: Acetyl-coa synthetase like fold]] | [[Category: Acetyl-coa synthetase like fold]] | ||
[[Category: Amp-binding]] | [[Category: Amp-binding]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
Revision as of 07:28, 21 December 2014
Crystal structure of N-terminal domain of FAAL28 G330W mutant from Mycobacterium tuberculosis
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