3qxe

Crystal Structure of Co-type Nitrile Hydratase from Pseudomonas putida.

spinqualitylabelsall models 3qxe, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qxe is a 8 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.104Å Ligands: 3CO, CSD, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Active sites may be regarded as layers of residues, whereby the residues that interact directly with substrate also interact with residues in a second shell and these in turn interact with residues in a third shell. These residues in the second and third layers may have distinct roles in maintaining the essential chemical properties of the first-shell catalytic residues, particularly their spatial arrangement relative to the substrate binding pocket, and their electrostatic and dynamic properties. The extent to which these remote residues participate in catalysis and precisely how they affect first-shell residues remains unexplored. To improve our understanding of the roles of second- and third-shell residues in catalysis, we used THEMATICS to identify residues in the second and third shells of the Co-type nitrile hydratase from Pseudomonas putida (ppNHase) that may be important for catalysis. Five of these predicted residues, and three additional, conserved residues that were not predicted, have been conservatively mutated, and their effects have been studied both kinetically and structurally. The eight residues have no direct contact with the active site metal ion or bound substrate. These results demonstrate that three of the predicted second-shell residues (alpha-Asp164, beta-Glu56, and beta-His147) and one predicted third-shell residue (beta-His71) have significant effects on the catalytic efficiency of the enzyme. One of the predicted residues (alpha-Glu168) and the three residues not predicted (alpha-Arg170, alpha-Tyr171, and beta-Tyr215) do not have any significant effects on the catalytic efficiency of the enzyme. Evidence of the Participation of Remote Residues in the Catalytic Activity of Co-Type Nitrile Hydratase from Pseudomonas putida.,Brodkin HR, Novak WR, Milne AC, D'Aquino JA, Karabacak NM, Goldberg IG, Agar JN, Payne MS, Petsko GA, Ondrechen MJ, Ringe D Biochemistry. 2011 Jun 7;50(22):4923-35. Epub 2011 May 12. PMID:21473592 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nitrile hydratase

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