Structural highlights
FunctionPublication Abstract from PubMedComprehending the molecular strategies employed by Mycobacterium tuberculosis (Mtb) in FAS-II regulation is of paramount significance in order to curb tuberculosis (TB) progression. Mtb employs two sets of dehydratases, namely HadAB and HadBC (beta-hydroxy acyl ACP dehydratase), for the regulation of the Fatty Acid Synthase (FAS-II) pathway. We have utilized the Sequence similarity network (SSN) to comprehend the presence of two copies of the dehydratase gene in Mtb. This analysis groups HadC and HadA in different clusters, which could be attributed to the variability in their physiological role with respect to the acyl chain uptake. Our study reveals structural details pertaining to the crystal structure of the last remaining enzyme of the FAS-II pathway. It provides insights into the highly flexible hot-dog helix (alpha-HD) and substrate regulatory loop. Additionally, mutational studies assisted in establishing the role of the C-terminal end in HadC of HadBC in the regulation of Acyl Carrier Protein (AcpM) mediated interactions. Complemented with SPR and MD simulation studies, this work provides the first evidence of the molecular mechanisms involved in the differential binding affinity of the AcpM towards both mtbHadAB and mtbHadBC. The C-terminal end of mycobacterial HadBC regulates AcpM interaction during the FAS-II pathway: a structural perspective.,Singh BK, Biswas R, Bhattacharyya S, Basak A, Das AK FEBS J. 2022 Feb 17. doi: 10.1111/febs.16405. PMID:35175661[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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