3dr2

Structural and Functional Analyses of XC5397 from Xanthomonas campestris: A Gluconolactonase Important in Glucose Secondary Metabolic Pathways

spinqualitylabelsall models 3dr2, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dr2 is a 2 chain structure with sequence from Xanthomonas campestris pv. campestris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.67Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B0RN69_XANCB Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The first gluconolactonase crystal structure from bacteria has been determined to a resolution of 1.61 A using X-ray crystallography. It belongs to the senescence marker protein 30/gluconolaconase superfamily but exhibits substrate specificity mainly toward D-glucono-delta-lactone. It forms a novel disulfide-bonded clamshell dimer comprising two doughnut-shaped six-bladed beta-propeller domains, yet with an exceptionally long N-terminal subdomain forming an extra helix and four additional beta-strands to enclose half of the outermost beta-strands of each propeller. Extensive interactions, including H-bonds, salt bridges, disulfide bonds, and coordination bonds, along with numerous bridging water molecules, are present in the interface to institute the "top-to-top" clamshell-type dimer. Three calcium ions per subunit were observed. Two are present in the central water-filled channel, with the top one coordinated to four highly conserved amino acids and is possibly involved in substrate hydrolysis, while the bottom one is coordinated to the backbone oxygen atoms, which is possibly for stabilizing the propeller domain. One calcium ion is situated in the interface also to stabilize the dimer form. Since gluconolactonase is essential in the glucose secondary metabolic pathways leading to the synthesis of pentose, vitamin C, or "antiaging" factors, determination of its tertiary structure should help understand these important biochemical processes. The first crystal structure of gluconolactonase important in the glucose secondary metabolic pathways.,Chen CN, Chin KH, Wang AH, Chou SH J Mol Biol. 2008 Dec 19;384(3):604-14. Epub 2008 Sep 30. PMID:18848569 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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