Uridylate kinase

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<StructureSection load='2j4k' size='340' side='right' caption='Uridylate kinase hexamer complex with ligand UMP (stick model), Cd+ (gold) and Mg+2 (green) ions [[2j4k]]' scene='' >
<StructureSection load='2j4k' size='340' side='right' caption='Uridylate kinase hexamer complex with ligand UMP (stick model), Cd+ (gold) and Mg+2 (green) ions [[2j4k]]' scene='' >
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== Function ==
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'''Uridylate kinase''' (UK) catalyzes the reversible transfer of phosphate from UMP to UDP using ATP as a phosphate source. UDP is the starting point of synthesis of all other pyrimidine nucleotides. The eukaryotic UK has specificity to both UMP and CMP while the bacterial one is specific for UMP. The bacterial UK is Mg+2 dependent and is activated by GTP and repressed by UTP. The bacterial UK is composed of a C terminal ATP-binding domain and an N terminal UMP-binding domain<ref>PMID:15454079</ref>.
'''Uridylate kinase''' (UK) catalyzes the reversible transfer of phosphate from UMP to UDP using ATP as a phosphate source. UDP is the starting point of synthesis of all other pyrimidine nucleotides. The eukaryotic UK has specificity to both UMP and CMP while the bacterial one is specific for UMP. The bacterial UK is Mg+2 dependent and is activated by GTP and repressed by UTP. The bacterial UK is composed of a C terminal ATP-binding domain and an N terminal UMP-binding domain<ref>PMID:15454079</ref>.
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== Structural highlights ==
</StructureSection>
</StructureSection>
==3D structures of uridylate kinase==
==3D structures of uridylate kinase==

Revision as of 08:43, 11 December 2016

Uridylate kinase hexamer complex with ligand UMP (stick model), Cd+ (gold) and Mg+2 (green) ions 2j4k

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3D structures of uridylate kinase

Updated on 11-December-2016

References

  1. ↑ Dhar G, Sanders ER, Johnson RC. Architecture of the hin synaptic complex during recombination: the recombinase subunits translocate with the DNA strands. Cell. 2004 Oct 1;119(1):33-45. PMID:15454079 doi:http://dx.doi.org/10.1016/j.cell.2004.09.010

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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