1TRI
THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP
Summary for 1TRI
Entry DOI | 10.2210/pdb1tri/pdb |
Descriptor | TRIOSEPHOSPHATE ISOMERASE, SULFATE ION (3 entities in total) |
Functional Keywords | isomerase(intramolecular oxidoreductase) |
Biological source | Trypanosoma brucei brucei |
Total number of polymer chains | 1 |
Total formula weight | 26188.90 |
Authors | Wierenga, R.K. (deposition date: 1993-10-08, release date: 1994-07-31, Last modification date: 2024-02-14) |
Primary citation | Borchert, T.V.,Abagyan, R.,Kishan, K.V.,Zeelen, J.P.,Wierenga, R.K. The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of an eight-residue loop. Structure, 1:205-213, 1993 Cited by PubMed Abstract: The triosephosphate isomerase (TIM) fold is found in several different classes of enzymes, most of which are oligomers; TIM itself always functions as a very tight dimer. It has recently been shown that a monomeric form of TIM ('monoTIM') can be constructed by replacing a 15-residue interface loop, loop-3, with an eight-residue fragment; modelling suggests that this should result in a short strain-free turn, resulting in the subsequent helix, helix-A3, having an additional turn at its amino terminus. PubMed: 16100954DOI: 10.1016/0969-2126(93)90021-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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