1nzc

The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose

spinqualitylabelsall models 1nzc, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nzc is a 4 chain structure with sequence from Streptococcus suis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: NI, TDX Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8GIQ0_STRSU 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 Nature achieves the epimerization of carbohydrates by a variety of chemical routes. One common route is that performed by the class of enzyme defined by dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC) from the rhamnose pathway. Earlier studies failed to identify the key residues in catalysis. We report the 1.3 A structure of RmlC from Streptococcus suis type 2 and its complexes with dTDP-D-glucose and dTDP-D-xylose. The streptococcal RmlC enzymes belong to a separate subgroup, sharing only 25% identity with RmlC from other bacteria, yet the S. suis enzyme has similar kinetic properties and structure to other RmlC enzymes. Structure, sequence alignment, and mutational analysis have now allowed reliable identification of the catalytic residues and their roles. High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme.,Dong C, Major LL, Allen A, Blankenfeldt W, Maskell D, Naismith JH Structure. 2003 Jun;11(6):715-23. PMID:12791259 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RmlC

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