Journal:Acta Cryst D:S2059798322001772
From Proteopedia
Crystal structure of the putative cell wall lipoglycan biosynthesis protein LmcA from Mycobacterium smegmatisOnisha Patel, Rajini Brammananth, Weiwen Dai, Santosh Panjikar, Ross L. Coppel, Isabelle S. Lucet and Paul K. Crellin [1] Molecular Tour The LmcA structure revealed an elongated beta-barrel fold and one alpha-helix extending away from the beta-barrel core. adopts an extended beta-barrel core composed of 11 antiparallel beta-strands with two alpha-turns and one alpha-helix extending away from the core. The secondary structure elements are shown in distinct colours. Interestingly, were found inside the protein which could bind a ligand. Further analysis revealed elements in LmcA that may undergo conformational changes to ‘open’ the protein, permitting access to the cavities. . . While the ligand remains to be identified, comparison of the crystal structure with LmcA models from other bacterial species suggests a common mechanism of ligand binding involving the cavities. These findings provide new structural insights into the biosynthetic pathway for PIM/LM/LAM, essential components of the mycobacterial cell surface. PDB references: MSMEG_0317Δ, 7n3v; xenon derivative, 7shw. References
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