4o7p

Crystal structure of Mycobacterium tuberculosis maltose kinase MaK complexed with maltose

spinqualitylabelsall models 4o7p, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4o7p is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BTB, GLC, PRD_900001, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MAK1_MYCTU Publication Abstract from PubMed Mycobacterium tuberculosis (Mtb) uses maltose-1-phosphate to synthesize alpha-glucans that make up the major component of its outer capsular layer. Maltose kinase (MaK) catalyzes phosphorylation of maltose. The molecular basis for this phosphorylation is currently not understood. Here, we describe the first crystal structure of MtbMaK refined to 2.4 A resolution. The bi-modular architecture of MtbMaK reveals a remarkably unique N-lobe. An extended sheet protrudes into ligand binding pocket of an adjacent monomer and contributes residues critical for kinase activity. Structure of the complex of MtbMaK bound with maltose reveals that maltose binds in a shallow cavity of the C-lobe. Structural constraints permit phosphorylation of alpha-maltose only. Surprisingly, instead of a Gly-rich loop, MtbMaK employs 'EQS' loop to tether ATP. Notably, this loop is conserved across all MaK homologues. Structures of MtbMaK presented here unveil features that are markedly different from other kinases and support the scaffolding role proposed for this kinase. Homotypic dimerization of a maltose kinase for molecular scaffolding.,Li J, Guan X, Shaw N, Chen W, Dong Y, Xu X, Li X, Rao Z Sci Rep. 2014 Sep 23;4:6418. doi: 10.1038/srep06418. PMID:25245657 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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