5oyn

Crystal structure of D-xylonate dehydratase in holo-form

spinqualitylabelsall models 5oyn, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5oyn is a 4 chain structure with sequence from Caulobacter vibrioides CB15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: FES, KCX, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function XYLD_CAUVC Catalyzes the dehydration of D-xylonate to 2-dehydro-3-deoxy-D-arabinonate during D-xylose degradation. Can also dehydrate D-gluconate, with similar catalytic efficiency. Has weak activity with D-galactonate, D-fuconate and L-arabinonate. Publication Abstract from PubMed The Ilv/ED dehydratase protein family includes dihydroxy acid-, gluconate-, 6-phosphogluconate- and pentonate dehydratases. The members of this family are involved in various biosynthetic and carbohydrate metabolic pathways. Here, we describe the first crystal structure of D-xylonate dehydratase from Caulobacter crescentus (CcXyDHT) at 2.7 A resolution and compare it with other available enzyme structures from the IlvD/EDD protein family. The quaternary structure of CcXyDHT is a tetramer, and each monomer is composed of two domains in which the N-terminal domain forms a binding site for a [2Fe-2S] cluster and a Mg(2+) ion. The active site is located at the monomer-monomer interface and contains residues from both the N-terminal recognition helix and the C-terminus of the dimeric counterpart. The active site also contains a conserved Ser490, which probably acts as a base in catalysis. Importantly, the cysteines that participate in the binding and formation of the [2Fe-2S] cluster are not all conserved within the Ilv/ED dehydratase family, which suggests that some members of the IlvD/EDD family may bind different types of [Fe-S] clusters. The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family.,Rahman MM, Andberg M, Koivula A, Rouvinen J, Hakulinen N Sci Rep. 2018 Jan 16;8(1):865. doi: 10.1038/s41598-018-19192-6. PMID:29339766 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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