1tev: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1tev.jpg|left|200px]] | [[Image:1tev.jpg|left|200px]] | ||
'''Crystal structure of the human UMP/CMP kinase in open conformation''' | {{Structure | ||
|PDB= 1tev |SIZE=350|CAPTION= <scene name='initialview01'>1tev</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Cytidylate_kinase Cytidylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.14 2.7.4.14] | |||
|GENE= UCK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal structure of the human UMP/CMP kinase in open conformation''' | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
1TEV is a [ | 1TEV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TEV OCA]. | ||
==Reference== | ==Reference== | ||
Substrate-induced conformational changes in human UMP/CMP kinase., Segura-Pena D, Sekulic N, Ort S, Konrad M, Lavie A, J Biol Chem. 2004 Aug 6;279(32):33882-9. Epub 2004 May 26. PMID:[http:// | Substrate-induced conformational changes in human UMP/CMP kinase., Segura-Pena D, Sekulic N, Ort S, Konrad M, Lavie A, J Biol Chem. 2004 Aug 6;279(32):33882-9. Epub 2004 May 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15163660 15163660] | ||
[[Category: Cytidylate kinase]] | [[Category: Cytidylate kinase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| Line 23: | Line 32: | ||
[[Category: Sekulic, N.]] | [[Category: Sekulic, N.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: conformational | [[Category: conformational change]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
[[Category: lid region]] | [[Category: lid region]] | ||
| Line 29: | Line 38: | ||
[[Category: ploop]] | [[Category: ploop]] | ||
''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 14:17:29 2008'' | ||
Revision as of 15:17, 20 March 2008
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | UCK (Homo sapiens) | ||||||
| Activity: | Cytidylate kinase, with EC number 2.7.4.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the human UMP/CMP kinase in open conformation
OverviewOverview
Human UMP/CMP kinase plays a crucial role in supplying precursors for nucleic acid synthesis by catalyzing the conversion of UMP, CMP, and dCMP into their diphosphate form. In addition, this kinase is an essential component of the activation cascade of medicinally relevant nucleoside analog prodrugs such as AraC, gemcitabine, and ddC. During the catalytic cycle the enzyme undergoes large conformational changes from open in the absence of substrates to closed in the presence of both phosphoryl donor and phosphoryl acceptor. Here we report the crystal structure of the substrate-free, open form of human UMP/CMP kinase. Comparison of the open structure with the closed state previously reported for the similar Dictyostelium discoideum UMP/CMP kinase reveals the conformational changes that occur upon substrate binding. We observe a classic example of induced fit where substrate-induced conformational changes in hinge residues result in rigid body movements of functional domains to form the catalytically competent state. In addition, a homology model of the human enzyme in the closed state based on the structure of D. discoideum UMP/CMP kinase aids to rationalize the substrate specificity of the human enzyme.
DiseaseDisease
Known disease associated with this structure: HIV infection, susceptibility/resistance to OMIM:[601267]
About this StructureAbout this Structure
1TEV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Substrate-induced conformational changes in human UMP/CMP kinase., Segura-Pena D, Sekulic N, Ort S, Konrad M, Lavie A, J Biol Chem. 2004 Aug 6;279(32):33882-9. Epub 2004 May 26. PMID:15163660
Page seeded by OCA on Thu Mar 20 14:17:29 2008