3stf | pdb_00003stf

Crystal structure of a mutant (S211A) of 3-deoxy-D-manno-octulosonate 8-phosphate synthase (KDO8PS) from Neisseria meningitidis

spinqualitylabelsall models 3stf, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3stf is a 4 chain structure with sequence from Neisseria meningitidis MC58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CL, GOL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KDSA_NEIMB Publication Abstract from PubMed The enzyme 3-deoxy-d-manno-octulosonate 8-phosphate (KDO8P) synthase catalyzes the reaction between phosphoenolpyruvate and arabinose 5-phosphate (A5P) in the first committed step in the biosynthetic pathway for the formation of 3-deoxy-d-manno-octulosonate, an important component in the cell wall of Gram-negative bacteria. KDO8P synthase is evolutionarily related to the first enzyme of the shikimate pathway, 3-deoxy-d-arabino-heptulosonate 7-phosphate (DAH7P) synthase, which uses erythrose 4-phosphate in place of A5P. The A5P binding site in KDO8P synthase is formed by three long loops that extend from the core catalytic (beta/alpha)(8) barrel, beta2alpha2, beta7alpha7, and beta8alpha8. The extended beta7alpha7 loop is always present in KDO8P synthase yet is not observed for DAH7P synthase. Modeling of this loop indicated interactions between this loop and the extended beta2alpha2 loop; both loops provide key hydrogen-bonding contacts with A5P. The two absolutely conserved residues on the beta7alpha7 loop (Gln and Ser) were mutated to Ala in both the metal-dependent KDO8P synthase from Acidithiobacillus ferrooxidans and the metal-independent KDO8P synthase from Neisseria meningitidis. In addition, mutants were constructed for both enzymes with the extended beta7alpha7 loop excised to match the DAH7P synthase architecture. Removal of the loop extension severely hindered efficient catalysis, dramatically increasing the K(m)(A5P) and reducing the k(cat) for both enzymes. Excision of the complete loop was far more detrimental to catalysis than the double mutations of the two conserved Gln and Ser residues. Therefore, the presence of the entire extended beta7alpha7 loop is important for efficient catalysis by KDO8P synthase, with the loop acting to promote efficient and productive binding of A5P. An Extended beta7alpha7 Substrate-Binding Loop Is Essential for Efficient Catalysis by 3-Deoxy-d-manno-Octulosonate 8-Phosphate Synthase.,Allison TM, Hutton RD, Jiao W, Gloyne BJ, Nimmo EB, Jameson GB, Parker EJ Biochemistry. 2011 Nov 1;50(43):9318-27. Epub 2011 Oct 10. PMID:21942786 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Kdo-8-phosphate synthase

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