Three-dimensional structure of the complex of guanylate kinase from yeast with its substrate GMP.
The enzyme guanylate kinase was isolated from baker's yeast and crystallized as a complex with its substrate GMP. The crystal structure was solved by multiple isomorphous replacement, solvent-flattening, restrained least-squares refinement, and simulated annealing. The current R-factor is 28.9% at a resolution of 2.0 A. The model is given as a backbone tracing, the GMP binding site is shown in atomic detail. In its major domain (residues 1 to 32 and 82 to 186), the chain fold is closely similar to the adenylate kinases, while the minor domain (residues 33 to 81) differs grossly from the 3-helix fold of the adenylate kinases. Structural homology and mechanistical similarity allow us to assign the AMP site of the adenylate kinases on the basis of the GMP site.
Stehle
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Institut für Organische Chemie und Biochemie der Universität, Frieburg, F.R.G.
Schulz
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GE
D001665:Binding Sites; D006150:Guanine Nucleotides / Q000378:metabolism*; D006157:Guanosine Monophosphate / Q000378:metabolism*; D006162:Guanylate Cyclase / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014961:X-Ray Diffraction / Q000379:methods
D006150:Guanine Nucleotides; D006157:Guanosine Monophosphate; D006162:Guanylate Cyclase