3t5a
From Proteopedia
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| - | {{STRUCTURE_3t5a| PDB=3t5a | SCENE= }} | ||
| - | ===Crystal structure of N-terminal domain of FAAL28 G330W mutant from Mycobacterium tuberculosis=== | ||
| - | {{ABSTRACT_PUBMED_22206988}} | ||
| - | == | + | ==Crystal structure of N-terminal domain of FAAL28 G330W mutant from Mycobacterium tuberculosis== |
| - | [[http://www.uniprot.org/uniprot/FAA28_MYCTU FAA28_MYCTU | + | <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 [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=3T5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T5A 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]] 2.05Å</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=3t5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5a OCA], [https://pdbe.org/3t5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t5a RCSB], [https://www.ebi.ac.uk/pdbsum/3t5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t5a ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FAA28_MYCTU FAA28_MYCTU] Catalyzes the activation of long-chain fatty acids (C22-24 fatty acids) as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase Mas for further chain extension. Involved in the biosynthesis of mycoserates.<ref>PMID:10573420</ref> <ref>PMID:11279114</ref> <ref>PMID:15042094</ref> | ||
| + | <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> |
| - | + | <div class="pdbe-citations 3t5a" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Mycobacterium tuberculosis H37Rv]] | ||
| + | [[Category: Goyal A]] | ||
| + | [[Category: Sankaranarayanan R]] | ||
Current revision
Crystal structure of N-terminal domain of FAAL28 G330W mutant from Mycobacterium tuberculosis
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