1ex7: Difference between revisions
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'''CRYSTAL STRUCTURE OF YEAST GUANYLATE KINASE IN COMPLEX WITH GUANOSINE-5'-MONOPHOSPHATE''' | {{Structure | ||
|PDB= 1ex7 |SIZE=350|CAPTION= <scene name='initialview01'>1ex7</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=5GP:GUANOSINE-5'-MONOPHOSPHATE'>5GP</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Guanylate_kinase Guanylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.8 2.7.4.8] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF YEAST GUANYLATE KINASE IN COMPLEX WITH GUANOSINE-5'-MONOPHOSPHATE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EX7 is a [ | 1EX7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EX7 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of unligated guanylate kinase from yeast reveals GMP-induced conformational changes., Blaszczyk J, Li Y, Yan H, Ji X, J Mol Biol. 2001 Mar 16;307(1):247-57. PMID:[http:// | Crystal structure of unligated guanylate kinase from yeast reveals GMP-induced conformational changes., Blaszczyk J, Li Y, Yan H, Ji X, J Mol Biol. 2001 Mar 16;307(1):247-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11243817 11243817] | ||
[[Category: Guanylate kinase]] | [[Category: Guanylate kinase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:29 2008'' | ||
Revision as of 12:01, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Guanylate kinase, with EC number 2.7.4.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF YEAST GUANYLATE KINASE IN COMPLEX WITH GUANOSINE-5'-MONOPHOSPHATE
OverviewOverview
The crystal structure of guanylate kinase (GK) from yeast (Saccharomyces cerevisiae) with a non-acetylated N terminus has been determined in its unligated form (apo-GK) as well as in complex with GMP (GK.GMP). The structure of apo-GK was solved with multiwavelength anomalous diffraction data and refined to an R-factor of 0.164 (R(free)=0.199) at 2.3 A resolution. The structure of GK.GMP was determined using the crystal structure of GK with an acetylated N terminus as the search model and refined to an R-factor of 0.156 (R(free)=0.245) at 1.9 A. GK belongs to the family of nucleoside monophosphate (NMP) kinases and catalyzes the reversible phosphoryl transfer from ATP to GMP. Like other NMP kinases, GK consists of three dynamic domains: the CORE, LID, and NMP-binding domains. Dramatic movements of the GMP-binding domain and smaller but significant movements of the LID domain have been revealed by comparing the structures of apo-GK and GK.GMP. apo-GK has a much more open conformation than the GK.GMP complex. Systematic analysis of the domain movements using the program DynDom shows that the large movements of the GMP-binding domain involve a rotation around an effective hinge axis approximately parallel with helix 3, which connects the GMP-binding and CORE domains. The C-terminal portion of helix 3, which connects to the CORE domain, has strikingly higher temperature factors in GK.GMP than in apo-GK, indicating that these residues become more mobile upon GMP binding. The results suggest that helix 3 plays an important role in domain movement. Unlike the GMP-binding domain, which moves toward the active center of the enzyme upon GMP binding, the LID domain moves away from the active center and makes the presumed ATP-binding site more open. Therefore, the LID domain movement may facilitate the binding of MgATP. The structure of the recombinant GK.GMP complex superimposes very well with that of the native GK.GMP complex, indicating that N-terminal acetylation does not have significant impact on the three-dimensional structure of GK.
About this StructureAbout this Structure
1EX7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of unligated guanylate kinase from yeast reveals GMP-induced conformational changes., Blaszczyk J, Li Y, Yan H, Ji X, J Mol Biol. 2001 Mar 16;307(1):247-57. PMID:11243817
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