1A3W

PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH FBP, PG, MN2+ AND K+

1A3W の概要

• エントリーDOI: 10.2210/pdb1a3w/pdb
• 分子名称: PYRUVATE KINASE, 2-PHOSPHOGLYCOLIC ACID, 1,6-di-O-phosphono-beta-D-fructofuranose, ... (5 entities in total)
• 機能のキーワード: pyruvate kinase, allosteric regulation, tranferase, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 110405.26

構造登録者

Jurica, M.S.,Mesecar, A.,Heath, P.J.,Shi, W.,Nowak, T.,Stoddard, B.L. (登録日: 1998-01-26, 公開日: 1998-05-27, 最終更新日: 2024-05-22)

主引用文献

Jurica, M.S.,Mesecar, A.,Heath, P.J.,Shi, W.,Nowak, T.,Stoddard, B.L.
The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate.
Structure, 6:195-210, 1998

PubMed Abstract: Yeast pyruvate kinase (PK) catalyzes the final step in glycolysis. The enzyme therefore represents an important control point and is allosterically activated by fructose-1,6-bisphosphate (FBP). In mammals the enzyme is found as four different isozymes with different regulatory properties: two of these isozymes are produced by alternate splicing. The allosteric regulation of PK is directly related to proliferation of certain cell types, as demonstrated by the expression of an allosterically regulated isozyme in tumor cells. A model for the allosteric transition from the inactive (T) state to the active (R) state has been proposed previously, but until now the FBP-binding site had not been identified.

PubMed: 9519410
DOI: 10.1016/S0969-2126(98)00021-5

実験手法

X-RAY DIFFRACTION (3 Å)