1aps
From Proteopedia
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'''THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS''' | '''THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS''' | ||
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[[Category: Saudek, V.]] | [[Category: Saudek, V.]] | ||
[[Category: Williams, R J.P.]] | [[Category: Williams, R J.P.]] | ||
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Revision as of 07:33, 2 May 2008
THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS
Overview
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.
About this Structure
1APS is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 10:33:39 2008
