1aps

THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS

spinqualitylabelsall models 1aps Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1aps is a 1 chain structure with sequence from Equus caballus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACYP2_HORSE Its physiological role is not yet clear. 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 We report here the complete determination of the solution structure of acylphosphatase, a small enzyme that catalyses the hydrolysis of organic acylphosphates, as determined by distance geometry methods based on nuclear magnetic resonance information. A non-standard strategy for the distance geometry calculations was used and is described here some detail. The five best structures were then refined by restrained energy minimization and molecular dynamics in order to explore the conformational space consistent with the experimental data. We address the question of whether the solution structure of acylphosphatase follows the general principles of protein structure, i.e. those learned from analysing crystal structures. Static and dynamic features are discussed in detail. An uncommon beta-alpha-beta motif, so far found only in procarboxypeptidase B and in an RNA-binding protein, is present in acylphosphatase. Three-dimensional structure of acylphosphatase. Refinement and structure analysis.,Pastore A, Saudek V, Ramponi G, Williams RJ J Mol Biol. 1992 Mar 20;224(2):427-40. PMID:1313885 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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