1KV5

Structure of Trypanosoma brucei brucei TIM with the salt-bridge-forming residue Arg191 mutated to Ser

Summary for 1KV5

• Entry DOI: 10.2210/pdb1kv5/pdb
• Descriptor: triosephosphate isomerase, glycosomal, 2-PHOSPHOGLYCOLIC ACID, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (6 entities in total)
• Functional Keywords: tim barrel, mutant, salt bridge, isomerase
• Biological source: Trypanosoma brucei brucei
• Cellular location: Glycosome: P04789
• Total number of polymer chains: 2
• Total formula weight: 54522.19

Authors

Kursula, I.,Partanen, S.,Lambeir, A.-M.,Wierenga, R.K. (deposition date: 2002-01-25, release date: 2002-03-29, Last modification date: 2023-08-16)

Primary citation

Kursula, I.,Partanen, S.,Lambeir, A.-M.,Wierenga, R.K.
The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis
FEBS Lett., 518:39-42, 2002

PubMed Abstract: Triosephosphate isomerase (TIM) has a conserved salt bridge 20 A away from both the active site and the dimer interface. In this study, four salt bridge mutants of Trypanosoma brucei brucei TIM were characterized. The folding and stability of the mutants are impaired compared to the wild-type enzyme. This salt bridge is part of a hydrogen bonding network which tethers the C-terminal beta7alpha7beta8alpha8 unit to the bulk of the protein. In the variants D227N, D227A, and R191S, this network is preserved, as can be deduced from the structure of the R191S variant. In the R191A variant, the side chain at position 191 cannot contribute to this network. Also the catalytic power of this variant is most affected.

PubMed: 11997014
DOI: 10.1016/S0014-5793(02)02639-X

Experimental method

X-RAY DIFFRACTION (1.65 Å)