4rv2: Difference between revisions

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 <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=4rv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rv2 RCSB], [http://www.ebi.ac.uk/pdbsum/4rv2 PDBsum]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Fatty acid biosynthesis type II in mycobacteria delivers the fatty acids required for mycolic acid synthesis. The pathway employs a unique maoC like beta-hydroxyacyl-ACP dehydratase HadAB or HadBC heterodimer in the third step of the elongation cycle. Here we report the crystal structure of the HadAB complex determined using a Pb-SIRAS method. Crystal structure aided with enzymatic study establishes the roles of HadA as a scaffolding component and HadB as a catalytic component together indispensable for the activity. The detailed structural analysis of HadAB in combination with MD simulation endorses the spatial orientation of the central hot-dog helix and the dynamic nature of its associated loop in regulation of substrate specificities in dehydratase/hydratase family enzymes.
+Crystal structure of dehydratase component HadAB complex of mycobacterial FAS-II pathway.,Biswas R, Dutta A, Dutta D, Hazra D, Banerjee DR, Basak A, Das AK Biochem Biophys Res Commun. 2015 Mar 6;458(2):369-74. doi:, 10.1016/j.bbrc.2015.01.119. Epub 2015 Feb 3. PMID:25656575<ref>PMID:25656575</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>