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[[Image:2ukd.gif|left|200px]]<br /><applet load="2ukd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ukd, resolution 2.2&Aring;" />
'''UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMP'''<br />


==Overview==
==UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMP==
UMP/CMP kinase from Dictyostelium discoideum (UmpKdicty) catalyzes the specific transfer of the terminal phosphate of ATP to UMP or CMP. Crystal structures of UmpKdicty with substrates and the transition state analogs AlF3 or BeF2 that lock UmpKdicty in active conformations were solved. The positions of the catalytic Mg2+ and the highly conserved lysine of the P loop are virtually invariant in the different structures. In contrast, catalytic arginines move to stabilize charges that develop during this reaction. The location of the arginines indicates formation of negative charges during the reaction at the transferred phosphoryl group, but not at the phosphate bridging oxygen atoms. This is consistent with an associative phosphoryl transfer mechanism but not with a dissociative one.
<StructureSection load='2ukd' size='340' side='right'caption='[[2ukd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ukd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UKD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ukd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ukd OCA], [https://pdbe.org/2ukd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ukd RCSB], [https://www.ebi.ac.uk/pdbsum/2ukd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ukd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KCY_DICDI KCY_DICDI] This UMP-CMP kinase uses preferentially ATP as phosphate donor and is specific for UMP and CMP.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uk/2ukd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ukd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2UKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=C5P:'>C5P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UKD OCA].
*[[UMP/CMP kinase|UMP/CMP kinase]]
 
__TOC__
==Reference==
</StructureSection>
Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative., Schlichting I, Reinstein J, Biochemistry. 1997 Aug 5;36(31):9290-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9280438 9280438]
[[Category: Cytidylate kinase]]
[[Category: Dictyostelium discoideum]]
[[Category: Dictyostelium discoideum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Reinstein, J.]]
[[Category: Reinstein J]]
[[Category: Schlichting, I.]]
[[Category: Schlichting I]]
[[Category: ADP]]
[[Category: C5P]]
[[Category: MG]]
[[Category: nmp kinase]]
[[Category: nucleoside monophosphate kinase]]
[[Category: phosphoryl transfer]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:13 2008''

Latest revision as of 12:24, 21 February 2024

UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMPUMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMP

Structural highlights

2ukd is a 1 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KCY_DICDI This UMP-CMP kinase uses preferentially ATP as phosphate donor and is specific for UMP and CMP.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2ukd, resolution 2.20Å

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