2E28

Crystal structure analysis of pyruvate kinase from Bacillus stearothermophilus

2E28 の概要

• エントリーDOI: 10.2210/pdb2e28/pdb
• 分子名称: Pyruvate kinase, SULFATE ION (3 entities in total)
• 機能のキーワード: pyruvate kinase, allosteric, transferase
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62458.59

構造登録者

Suzuki, K. (登録日: 2006-11-09, 公開日: 2008-02-05, 最終更新日: 2023-10-25)

主引用文献

Suzuki, K.,Ito, S.,Shimizu-Ibuka, A.,Sakai, H.
Crystal structure of pyruvate kinase from Geobacillus stearothermophilus.
J.Biochem., 144:305-312, 2008

PubMed Abstract: The pyruvate kinase (PK) from a moderate thermophile, Geobacillus stearothermophilus, is an allosteric enzyme activated by AMP and ribose 5-phosphate but not fructose 1, 6-bisphosphate (FBP), which is a common activator of PKs. It has an extra C-terminal sequence (ECTS), which contains a highly conserved phosphoenolpyruvate (PEP) binding motif, but its function and structure remain unclear. To elucidate the structural characteristics of the effector-binding site and the ECTS, the crystal structure of the C9S/C268S mutant of the enzyme was determined at 2.4 A resolution. The crystal belonged to space group P6(2)22, with unit cell parameters a, b = 145.97 A, c = 118.03 A. The enzyme was a homotetramer and its overall domain structure was similar to the previously solved structures except that the ECTS formed a new domain (C' domain). The structure of the C' domain closely resembled that of the PEP binding domain of maize pyruvate phosphate dikinase. A sulphate ion was found in a pocket in the effector-binding C domain. This site corresponds to the 6-phosphate group-binding site in yeast PK bound FBP and seems to be the effector-binding site. Through comparison of the structure of the putative effector-binding site to that of the FBP binding site of the yeast enzyme, the structural basis of the effector specificity of the G. stearothermophilus PK is discussed.

PubMed: 18511452
DOI: 10.1093/jb/mvn069

実験手法

X-RAY DIFFRACTION (2.4 Å)