1TTI

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

Summary for 1TTI

• Entry DOI: 10.2210/pdb1tti/pdb
• Descriptor: TRIOSEPHOSPHATE ISOMERASE, 2-PHOSPHOGLYCOLIC ACID (3 entities in total)
• Functional Keywords: isomerase(intramolecular oxidoreductase)
• Biological source: Trypanosoma brucei brucei
• Total number of polymer chains: 1
• Total formula weight: 26349.97

Authors

Radha Kishan, K.V.,Wierenga, R.K. (deposition date: 1995-04-19, release date: 1995-10-15, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)