Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution - PubMed (original) (raw)
Comparative Study
. 1992 Apr 20;224(4):1127-41.
doi: 10.1016/0022-2836(92)90474-x.
Affiliations
- PMID: 1314905
- DOI: 10.1016/0022-2836(92)90474-x
Comparative Study
Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution
T Stehle et al. J Mol Biol. 1992.
Abstract
The crystal structure of guanylate kinase from Saccharomyces cerevisiae complexed with its substrate GMP has been refined at a resolution of 2.0 A. The final crystallographic R-factor is 17.3% in the resolution range 7.0 A to 2.0 A for all reflections of the 100% complete data set. The final model has standard geometry with root-mean-square deviations of 0.016 A in bond lengths and 3.0 in bond angles. It consists of all 186 amino acid residues, the N-terminal acetyl group, the substrate GMP, one sulfate ion and 174 water molecules. Guanylate kinase is structurally related to adenylate kinases and G-proteins with respect to its central beta-sheet with connecting helices and the giant anion hole that binds nucleoside triphosphates. These nucleotides are ATP and GTP for the kinases and GTP for the G-proteins. The chain segment binding the substrate GMP of guanylate kinase differs grossly from the respective part of the adenylate kinases; it has no counterpart in the G-proteins. The binding mode of GMP is described in detail. Probably, the observed structure represents one of several structurally quite different intermediate states of the catalytic cycle.
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