1TTJ

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

Summary for 1TTJ

Entry DOI	10.2210/pdb1ttj/pdb
Descriptor	TRIOSEPHOSPHATE ISOMERASE, PHOSPHOGLYCOLOHYDROXAMIC ACID (3 entities in total)
Functional Keywords	isomerase(intramolecular oxidoreductase)
Biological source	Trypanosoma brucei brucei
Total number of polymer chains	1
Total formula weight	26191.73
Authors	Radha Kishan, K.V.,Wierenga, R.K. (deposition date: 1995-04-20, release date: 1995-09-15, 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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.4 Å)

Structure validation