5cim

Structure of Mycobacterium thermoresistibile GlgE in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution

spinqualitylabelsall models 5cim, resolution 3.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cim is a 2 chain structure with sequence from Mycolicibacterium thermoresistibile ATCC 19527. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.32Å Ligands: GLC, PRD_900001 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G7CL00_MYCT3 Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.[HAMAP-Rule:MF_02124] Publication Abstract from PubMed GlgE, an enzyme of the pathway that converts trehalose to alpha-glucans, is essential for Mycobacterium tuberculosis. Inhibition of GlgE, which transfers maltose from a maltose-1-phosphate donor to alpha-glucan/maltooligosaccharide chain acceptor, leads to a toxic accumulation of maltose-1-phosphate that culminates in cellular death. Here we describe the first high-resolution mycobacterial GlgE structure from Mycobacterium thermoresistibile at 1.96 A. We show that the structure resembles that of M. tuberculosis and Streptomyces coelicolor GlgEs, reported before, with each protomer in the homodimer comprising five domains. However, in M. thermoresistibile GlgE we observe several conformational states of the S domain and provide evidence that its high flexibility is important for enzyme activity. The structures here reported shed further light on the interactions between the N-terminal domains and the catalytic domains of opposing chains and how they contribute to the catalytic reaction. Importantly this work identifies a useful surrogate system to aid the development of GlgE inhibitors against opportunistic and pathogenic mycobacteria. Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.,Mendes V, Blaszczyk M, Maranha A, Empadinhas N, Blundell TL Sci Rep. 2015 Nov 30;5:17144. doi: 10.1038/srep17144. PMID:26616850 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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