2psp
From Proteopedia
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PORCINE PANCREATIC SPASMOLYTIC POLYPEPTIDE
Overview
The structure of a trigonal crystal form of porcine pancreatic spasmolytic, polypeptide (PSP) has been solved by molecular replacement and refined to, 1.95 A resolution. Three heavy-atom derivatives were prepared, giving, unbiased phase information, which was used in the model building of the, protein molecules. The final conventional R value is 19.8% with the, inclusion of 183 water molecules. PSP crystallizes as a dimer in space, group P3(1)21 with a non-crystallographic twofold axis relating the, monomers. The monomer consists of two very similar domains each composed, of three loop regions. Two clefts are found in the monomer, one in each, domain, that are proposed as possible substrate-binding sites. Important, interactions have been identified in the proposed substrate-binding sites, where conserved water molecules probably mimic the hydrophilic positions, of the substrate. The estimated cleft size is 9 x 9 x 12 A. Analysis of, the charge distribution within the clefts, by an electrostatic potential, calculation, shows the clefts to be essentially non-charged.
About this Structure
2PSP is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Structure of porcine pancreatic spasmolytic polypeptide at 1.95 A resolution., Petersen TN, Henriksen A, Gajhede M, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):730-7. PMID:15299636
Page seeded by OCA on Wed Nov 21 13:39:19 2007
