|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1kdr' size='340' side='right'caption='[[1kdr]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='1kdr' size='340' side='right'caption='[[1kdr]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kdr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KDR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kdr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KDR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAR:CYTOSINE+ARABINOSE-5-PHOSPHATE'>CAR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kdo|1kdo]], [[1kdp|1kdp]], [[1kdt|1kdt]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAR:CYTOSINE+ARABINOSE-5-PHOSPHATE'>CAR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cmk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1kdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdr OCA], [https://pdbe.org/1kdr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kdr RCSB], [https://www.ebi.ac.uk/pdbsum/1kdr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kdr ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UMP/CMP_kinase UMP/CMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.14 2.7.4.14] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdr OCA], [http://pdbe.org/1kdr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kdr RCSB], [http://www.ebi.ac.uk/pdbsum/1kdr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kdr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KCY_ECOLI KCY_ECOLI]] ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.<ref>PMID:8190075</ref> <ref>PMID:7836281</ref> | + | [https://www.uniprot.org/uniprot/KCY_ECOLI KCY_ECOLI] ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.<ref>PMID:8190075</ref> <ref>PMID:7836281</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 38: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: UMP/CMP kinase]]
| + | [[Category: Assairi L]] |
| - | [[Category: Assairi, L]] | + | [[Category: Barzu O]] |
| - | [[Category: Barzu, O]] | + | [[Category: Bertrand T]] |
| - | [[Category: Bertrand, T]] | + | [[Category: Briozzo P]] |
| - | [[Category: Briozzo, P]] | + | [[Category: Bucurenci N]] |
| - | [[Category: Bucurenci, N]] | + | [[Category: Gilles AM]] |
| - | [[Category: Gilles, A M]] | + | [[Category: Golinelli-Pimpaneau B]] |
| - | [[Category: Golinelli-Pimpaneau, B]] | + | [[Category: Munier-Lehmann H]] |
| - | [[Category: Munier-Lehmann, H]] | + | [[Category: Ofiteru A]] |
| - | [[Category: Ofiteru, A]] | + | |
| - | [[Category: Nucleotide monophosphate kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
KCY_ECOLI ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacterial cytidine monophosphate (CMP) kinases are characterised by an insert enlarging their CMP binding domain, and by their particular substrate specificity. Thus, both CMP and 2'-deoxy-CMP (dCMP) are good phosphate acceptors for the CMP kinase from Escherichia coli (E. coli CMPK), whereas eukaryotic UMP/CMP kinases phosphorylate the deoxynucleotides with very low efficiency. Four crystal structures of E. coli CMPK complexed with nucleoside monophosphates differing in their sugar moiety were solved. Both structures with CMP or dCMP show interactions with the pentose that were not described so far. These interactions are lost with the poorer substrates AraCMP and 2',3'-dideoxy-CMP. Comparison of all four structures shows that the pentose hydroxyls are involved in ligand-induced movements of enzyme domains. It also gives a structural basis of the mechanism by which either ribose or deoxyribose can be accommodated. In parallel, for the four nucleotides the kinetic results of the wild-type enzyme and of three structure-based variants are presented. The phosphorylation rate is significantly decreased when either of the two pentose interacting residues is mutated. One of these is an arginine that is highly conserved in all known nucleoside monophosphate kinases. In contrast, the other residue, Asp185, is typical of bacterial CMP kinases. It interacts with Ser101, the only residue conserved in all CMP binding domain inserts. Mutating Ser101 reduces CMP phosphorylation only moderately, but dramatically reduces dCMP phosphorylation. This is the first experimental evidence of a catalytic role involving the characteristic insert of bacterial CMP kinases. Furthermore, this role concerns only dCMP phosphorylation, a feature of this family of enzymes.
Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme.,Bertrand T, Briozzo P, Assairi L, Ofiteru A, Bucurenci N, Munier-Lehmann H, Golinelli-Pimpaneau B, Barzu O, Gilles AM J Mol Biol. 2002 Feb 1;315(5):1099-110. PMID:11827479[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yamanaka K, Ogura T, Koonin EV, Niki H, Hiraga S. Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli. Mol Gen Genet. 1994 Apr;243(1):9-16. PMID:8190075
- ↑ Fricke J, Neuhard J, Kelln RA, Pedersen S. The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate in Escherichia coli. J Bacteriol. 1995 Feb;177(3):517-23. PMID:7836281
- ↑ Bertrand T, Briozzo P, Assairi L, Ofiteru A, Bucurenci N, Munier-Lehmann H, Golinelli-Pimpaneau B, Barzu O, Gilles AM. Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme. J Mol Biol. 2002 Feb 1;315(5):1099-110. PMID:11827479 doi:10.1006/jmbi.2001.5286
|
