4i3g | pdb_00004i3g

Crystal Structure of DesR, a beta-glucosidase from Streptomyces venezuelae in complex with D-glucose.

spinqualitylabelsall models 4i3g, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4i3g is a 2 chain structure with sequence from Streptomyces venezuelae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, EDO, MPO, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C5IXN7_STRVZ Publication Abstract from PubMed Antibiotics have, indeed, altered the course of human history as is evidenced by the increase in human life expectancy since the 1940s. Many of these natural compounds are produced by bacteria that, by necessity, must have efficient self-resistance mechanisms. The methymycin/pikromycin producing species Streptomyces venezuelae, for example, utilizes beta-glucosylation of its macrolide products to neutralize their effects within the confines of the cell. Once released into the environment, these compounds are activated by the removal of the glucose moiety. In S. venezuelae, the enzyme responsible for removal of the sugar from the parent compound is encoded by the desR gene and referred to as DesR. It is a secreted enzyme containing 828 amino acid residues, and it is known to be a retaining glycosidase. Here, we describe the structure of the DesR/D-glucose complex determined to 1.4-A resolution. The overall architecture of the enzyme can be envisioned in terms of three regions: a catalytic core and two auxiliary domains. The catalytic core harbors the binding platform for the glucose ligand. The first auxiliary domain adopts a "PA14 fold," whereas the second auxiliary domain contains an immunoglobulin-like fold. Asp 273 and Glu 578 are in the proper orientation to function as the catalytic base and proton donor, respectively, required for catalysis. The overall fold of the core region places DesR into the GH3 glycoside hydrolase family of enzymes. Comparison of the DesR structure with the beta-glucosidase from Kluyveromyces marxianus shows that their PA14 domains assume remarkably different orientations. The structure of DesR from Streptomyces venezuelae, a beta-glucosidase involved in macrolide activation.,Zmudka MW, Thoden JB, Holden HM Protein Sci. 2012 Dec 6. doi: 10.1002/pro.2204. PMID:23225731 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-glucosidase 3D structures

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