1TTI

THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8

1TTI の概要

• エントリーDOI: 10.2210/pdb1tti/pdb
• 分子名称: TRIOSEPHOSPHATE ISOMERASE, 2-PHOSPHOGLYCOLIC ACID (3 entities in total)
• 機能のキーワード: isomerase(intramolecular oxidoreductase)
• 由来する生物種: Trypanosoma brucei brucei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26349.97

構造登録者

Radha Kishan, K.V.,Wierenga, R.K. (登録日: 1995-04-19, 公開日: 1995-10-15, 最終更新日: 2024-02-14)

主引用文献

Borchert, T.V.,Kishan, K.V.,Zeelen, J.P.,Schliebs, W.,Thanki, N.,Abagyan, R.,Jaenicke, R.,Wierenga, R.K.
Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8.
Structure, 3:669-679, 1995

PubMed Abstract: Wild-type triosephosphate isomerase (TIM) is a very stable dimeric enzyme. This dimer can be converted into a stable monomeric protein (monoTIM) by replacing the 15-residue interface loop (loop-3) by a shorter, 8-residue, loop. The crystal structure of monoTIM shows that two active-site loops (loop-1 and loop-4), which are at the dimer interface in wild-type TIM, have acquired rather different structural properties. Nevertheless, monoTIM has residual catalytic activity.

PubMed: 8591044
DOI: 10.1016/S0969-2126(01)00202-7

実験手法

X-RAY DIFFRACTION (2.4 Å)