1N55

0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate

1N55 の概要

• エントリーDOI: 10.2210/pdb1n55/pdb
• 関連するPDBエントリー: 1IF2 1QDS
• 分子名称: triosephosphate isomerase, 2-PHOSPHOGLYCOLIC ACID, ACETIC ACID, ... (5 entities in total)
• 機能のキーワード: tim, atomic resolution, enzyme-ligand complex, transition-state analogue, low-barrier hydrogen bond, isomerase
• 由来する生物種: Leishmania mexicana
• 細胞内の位置: Cytoplasm: P48499
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27760.65

構造登録者

Kursula, I.,Wierenga, R.K. (登録日: 2002-11-04, 公開日: 2003-01-21, 最終更新日: 2024-02-14)

主引用文献

Kursula, I.,Wierenga, R.K.
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution
J.Biol.Chem., 278:9544-9551, 2003

PubMed Abstract: The atomic resolution structure of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate shows that this transition state analogue is bound in two conformations. Also for the side chain of the catalytic glutamate, Glu(167), two conformations are observed. In both conformations, a very short hydrogen bond exists between the carboxylate group of the ligand and the catalytic glutamate. The distance between O11 of PGA and Oepsilon2 of Glu(167) is 2.61 and 2.55 A for the major and minor conformations, respectively. In either conformation, Oepsilon1 of Glu(167) is hydrogen-bonded to a water network connecting the side chain with bulk solvent. This network also occurs in two mutually exclusive arrangements. Despite the structural disorder in the active site, the C termini of the beta strands that construct the active site display the least anisotropy compared with the rest of the protein. The loops following these beta strands display various degrees of anisotropy, with the tip of the dimer interface loop 3 having very low anisotropy and the C-terminal region of the active site loop 6 having the highest anisotropy. The pyrrolidine ring of Pro(168) at the N-terminal region of loop 6 is in a strained planar conformation to facilitate loop opening and product release.

PubMed: 12522213
DOI: 10.1074/jbc.M211389200

実験手法

X-RAY DIFFRACTION (0.83 Å)