4rv2
Crystal Structure of (3R)-hydroxyacyl-ACP dehydratase HadAB hetero-dimer from Mycobacterium smegmatisCrystal Structure of (3R)-hydroxyacyl-ACP dehydratase HadAB hetero-dimer from Mycobacterium smegmatis
Structural highlights
Publication Abstract from PubMedFatty 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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