1MSS

LARGE SCALE STRUCTURAL REARRANGEMENTS OF THE FRONT LOOPS IN MONOMERISED TRIOSEPHOSPHATE ISOMERASE, AS DEDUCED FROM THE COMPARISON OF THE STRUCTURAL PROPERTIES OF MONOTIM AND ITS POINT MUTATION VARIANT MONOSS

1MSS の概要

• エントリーDOI: 10.2210/pdb1mss/pdb
• 分子名称: TRIOSEPHOSPHATE ISOMERASE (2 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: 2
• 化学式量合計: 52041.38

構造登録者

Radha Kishan, K.V.,Wierenga, R.K. (登録日: 1994-07-27, 公開日: 1994-09-30, 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)