4RV2
Crystal Structure of (3R)-hydroxyacyl-ACP dehydratase HadAB hetero-dimer from Mycobacterium smegmatis
Summary for 4RV2
| Entry DOI | 10.2210/pdb4rv2/pdb |
| Descriptor | UPF0336 protein MSMEG_1340/MSMEI_1302, MaoC family protein, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | hotdog fold, lyase |
| Biological source | Mycobacterium smegmatis str. MC2 155 More |
| Total number of polymer chains | 2 |
| Total formula weight | 31460.38 |
| Authors | Biswas, R.,Hazra, D.,Dutta, D.,Das, A.K. (deposition date: 2014-11-24, release date: 2015-02-11, Last modification date: 2024-02-28) |
| Primary citation | Biswas, R.,Dutta, A.,Dutta, D.,Hazra, D.,Banerjee, D.R.,Basak, A.,Das, A.K. Crystal structure of dehydratase component HadAB complex of mycobacterial FAS-II pathway. Biochem.Biophys.Res.Commun., 458:369-374, 2015 Cited by PubMed Abstract: Fatty acid biosynthesis type II in mycobacteria delivers the fatty acids required for mycolic acid synthesis. The pathway employs a unique maoC like β-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. PubMed: 25656575DOI: 10.1016/j.bbrc.2015.01.119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
