1GKY

REFINED STRUCTURE OF THE COMPLEX BETWEEN GUANYLATE KINASE AND ITS SUBSTRATE GMP AT 2.0 ANGSTROMS RESOLUTION

Summary for 1GKY

• Entry DOI: 10.2210/pdb1gky/pdb
• Descriptor: GUANYLATE KINASE, SULFATE ION, GUANOSINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 21018.47

Authors

Stehle, T.,Schulz, G.E. (deposition date: 1991-12-23, release date: 1994-01-31, Last modification date: 2024-10-30)

Primary citation

Stehle, T.,Schulz, G.E.
Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution.
J.Mol.Biol., 224:1127-1141, 1992

PubMed 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.

PubMed: 1314905
DOI: 10.1016/0022-2836(92)90474-X

Experimental method

X-RAY DIFFRACTION (2 Å)