3zt7

GLGE ISOFORM 1 FROM STREPTOMYCES COELICOLOR WITH BETA-CYCLODEXTRIN AND MALTOSE BOUND

spinqualitylabelsall models 3zt7, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zt7 is a 4 chain structure with sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCD, MAL Related: 3zst, 3zss, 3zt6, 3zt5 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed GlgE is a recently identified (1-->4)-alpha-D-glucan:phosphate alpha-D-maltosyltransferase involved in alpha-glucan biosynthesis in bacteria and is a genetically validated anti-tuberculosis drug target. It is a member of the GH13_3 CAZy sub-family for which no structures were previously known. We have solved the structure of GlgE isoform I from Streptomyces coelicolor and shown that this enzyme has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. The S. coelicolor enzyme forms a homodimer with each subunit comprising five domains including a core catalytic alpha-amylase-type domain A with a (beta/alpha)8 fold. This domain is elaborated with domain B and two inserts that are specifically configured to define a well conserved donor pocket capable of binding maltose. Domain A, together with domain N from the neighbouring subunit, forms a hydrophobic patch that is close to the maltose binding site and capable of binding cyclodextrins. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, showing that the hydrophobic patch overlaps with the acceptor binding site. This patch is incompletely conserved in the M. tuberculosis enzyme such that cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. The crystal structure reveals two further domains, C and S, the latter being a helix bundle not previously reported in GH13 members. The structure provides a framework for understanding how GlgE functions and will help guide the development of inhibitors with therapeutic potential. Structure of a Streptomyces maltosyltransferase GlgE: a homologue of a genetically validated anti-tuberculosis target.,Syson K, Stevenson CE, Rejzek M, Fairhurst SA, Nair A, Bruton CJ, Field RA, Chater KF, Lawson DM, Bornemann S J Biol Chem. 2011 Sep 13. PMID:21914799 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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