2ZCI

Structure of a GTP-dependent bacterial PEP-carboxykinase from Corynebacterium glutamicum

2ZCI の概要

• エントリーDOI: 10.2210/pdb2zci/pdb
• 分子名称: Phosphoenolpyruvate carboxykinase [GTP] (2 entities in total)
• 機能のキーワード: gtp-dependent, carboxykinase, signaling protein, lyase
• 由来する生物種: Corynebacterium glutamicum
• 細胞内の位置: Cytoplasm (By similarity): Q9AEM1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 267748.47

構造登録者

Aich, S.,Prasad, L.,Delbaere, L.T.J. (登録日: 2007-11-09, 公開日: 2008-04-15, 最終更新日: 2023-08-30)

主引用文献

Aich, S.,Prasad, L.,Delbaere, L.T.
Structure of a GTP-dependent bacterial PEP-carboxykinase from Corynebacterium glutamicum.
Int.J.Biochem.Cell Biol., 40:1597-1603, 2008

PubMed Abstract: GTP-dependent phosphoenolpyruvate carboxykinase (PCK) is the key enzyme that controls the blood glucose level during fasting in higher animals. Here we report the first substrate-free structure of a GTP-dependent phosphoenolpyruvate (PEP) carboxykinase from a bacterium, Corynebacterium glutamicum (CgPCK). The protein crystallizes in space group P2(1) with four molecules per asymmetric unit. The 2.3A resolution structure was solved by molecular replacement using the human cytosolic PCK (hcPCK) structure (PDB ID: 1KHF) as the starting model. The four molecules in the asymmetric unit pack as two dimers, and is an artifact of crystal packing. However, the P-loop and the guanine binding loop of the substrate-free CgPCK structure have different conformations from the other published GTP-specific PCK structures, which all have bound substrates and/or metal ions. It appears that a change in the P-loop and guanine binding loop conformation is necessary for substrate binding in GTP-specific PCKs, as opposed to overall domain movement in ATP-specific PCKs.

PubMed: 18234538
DOI: 10.1016/j.biocel.2007.12.002

実験手法

X-RAY DIFFRACTION (2.3 Å)