1uei
From Proteopedia
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|PDB= 1uei |SIZE=350|CAPTION= <scene name='initialview01'>1uei</scene>, resolution 2.60Å | |PDB= 1uei |SIZE=350|CAPTION= <scene name='initialview01'>1uei</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=UTP:URIDINE 5'-TRIPHOSPHATE'>UTP</scene> | + | |LIGAND= <scene name='pdbligand=UTP:URIDINE+5'-TRIPHOSPHATE'>UTP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Uridine_kinase Uridine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.48 2.7.1.48] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_kinase Uridine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.48 2.7.1.48] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1udw|1UDW]], [[1uej|1UEJ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uei OCA], [http://www.ebi.ac.uk/pdbsum/1uei PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uei RCSB]</span> | ||
}} | }} | ||
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[[Category: Matsuda, A.]] | [[Category: Matsuda, A.]] | ||
[[Category: Suzuki, N N.]] | [[Category: Suzuki, N N.]] | ||
| - | [[Category: UTP]] | ||
[[Category: alpha/beta mononucleotide-binding hold]] | [[Category: alpha/beta mononucleotide-binding hold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:09:13 2008'' |
Revision as of 21:09, 30 March 2008
| |||||||
| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Uridine kinase, with EC number 2.7.1.48 | ||||||
| Related: | 1UDW, 1UEJ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human uridine-cytidine kinase 2 complexed with a feedback-inhibitor, UTP
Overview
Uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine and cytidine and activates pharmacological ribonucleoside analogs. Here we present the crystal structures of human UCK alone and in complexes with a substrate, cytidine, a feedback inhibitor, CTP or UTP, and with phosphorylation products, CMP and ADP, respectively. Free UCK takes an alpha/beta mononucleotide binding fold and exists as a homotetramer with 222 symmetry. Upon inhibitor binding, one loop region was loosened, causing the UCK tetramer to be distorted. Upon cytidine binding, a large induced fit was observed at the uridine/cytidine binding site, which endows UCK with a strict specificity for pyrimidine ribonucleosides. The first UCK structure provided the structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase, which give clues for the design of novel antitumor and antiviral ribonucleoside analogs that inhibit RNA synthesis.
About this Structure
1UEI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase., Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F, Structure. 2004 May;12(5):751-64. PMID:15130468
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