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

Summary for 1MSS

• Entry DOI: 10.2210/pdb1mss/pdb
• Descriptor: TRIOSEPHOSPHATE ISOMERASE (2 entities in total)
• Functional Keywords: isomerase(intramolecular oxidoreductase)
• Biological source: Trypanosoma brucei brucei
• Total number of polymer chains: 2
• Total formula weight: 52041.38

Authors

Radha Kishan, K.V.,Wierenga, R.K. (deposition date: 1994-07-27, release date: 1994-09-30, 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)