1FW8

CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72

1FW8 の概要

• エントリーDOI: 10.2210/pdb1fw8/pdb
• 分子名称: Phosphoglycerate kinase, GLYCEROL (3 entities in total)
• 機能のキーワード: phosphotransferase, kinase, phosphoglycerate kinase, glycolysis, mutant, permutation, permuted sequence, pgk, protein folding, two-domain protein, transferase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Cytoplasm : P00560
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45022.50

構造登録者

Tougard, P.,Bizebard, T.,Ritco-Vonsovici, M.,Minard, P.,Desmadril, M. (登録日: 2000-09-22, 公開日: 2001-03-22, 最終更新日: 2024-11-13)

主引用文献

Tougard, P.,Bizebard, T.,Ritco-Vonsovici, M.,Minard, P.,Desmadril, M.
Structure of a circularly permuted phosphoglycerate kinase.
Acta Crystallogr.,Sect.D, 58:2018-2023, 2002

PubMed Abstract: 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.

PubMed: 12454459
DOI: 10.1107/S0907444902015548

実験手法

X-RAY DIFFRACTION (2.3 Å)