1fw8

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spinqualitylabelsall models 1fw8, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72

Overview

The crystallographic structure of a circularly permuted form of yeast PGK, 72p yPGK, has been determined to a resolution of 2.3 A by molecular, replacement. In this engineered protein, the C- and N-terminal residues of, the wild-type protein are directly connected by a peptide bond and new N-, and C-terminal residues are located within the N-terminal domain. The, overall fold of the protein is very similar to that of the wild-type, protein, directly demonstrating that the continuity of a folding unit is, not relevant to the folding process of the whole protein. Only limited, structural changes were observed: these were in the regions associated, with the new connection, in a long flexible loop in the permuted domain, and in the vicinity of Arg38, a functionally important residue. The, relative positions of the two domains suggested that this permuted protein, adopts one of the most open/twisted conformations seen amongst PGKs of, known structure. The effect of the mutation on the functional properties, is more easily accounted for by a restriction of hinge-bending motion than, by structural changes in the protein.

About this Structure

1FW8 is a Single protein structure of sequence from Saccharomyces cerevisiae with ACE and GOL as ligands. Active as Phosphoglycerate kinase, with EC number 2.7.2.3 Full crystallographic information is available from OCA.

Reference

Structure of a circularly permuted phosphoglycerate kinase., Tougard P, Bizebard T, Ritco-Vonsovici M, Minard P, Desmadril M, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2018-23. Epub 2002, Nov 23. PMID:12454459

Page seeded by OCA on Tue Nov 20 15:22:04 2007