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| | <StructureSection load='3asy' size='340' side='right'caption='[[3asy]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3asy' size='340' side='right'caption='[[3asy]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3asy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ASY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ASY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3asy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ASY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ASY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3asz|3asz]]</div></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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">udk, TTHA0578 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Uridine_kinase Uridine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.48 2.7.1.48] </span></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=3asy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asy OCA], [https://pdbe.org/3asy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asy RCSB], [https://www.ebi.ac.uk/pdbsum/3asy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asy ProSAT]</span></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=3asy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asy OCA], [https://pdbe.org/3asy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asy RCSB], [https://www.ebi.ac.uk/pdbsum/3asy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/URK_THET8 URK_THET8] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet8]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Uridine kinase]]
| + | [[Category: Kuramitsu S]] |
| - | [[Category: Kuramitsu, S]] | + | [[Category: Masui R]] |
| - | [[Category: Masui, R]] | + | [[Category: Nakagawa N]] |
| - | [[Category: Nakagawa, N]] | + | [[Category: Tomoike F]] |
| - | [[Category: Tomoike, F]] | + | |
| - | [[Category: Cytidine phosphorylation]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
URK_THET8
Publication Abstract from PubMed
The salvage pathways of nucleotide biosynthesis are more diverse and are less well understood as compared with de novo pathways. Uridine-cytidine kinase (UCK) is the rate-limiting enzyme in the pyrimidine-nucleotide salvage pathway. In this study, we have characterized a UCK homologue of Thermus thermophilus HB8 (ttCK) biochemically and structurally. Unlike other UCKs, ttCK had substrate specificity toward only cytidine and showed no inhibition by UTP, suggesting uridine does not bind to ttCK as substrate. Structural analysis revealed that the histidine residue located near the functional group at position 4 of cytidine or uridine in most UCKs is substituted with tyrosine, Tyr93, in ttCK. Replacement of Tyr93 by histidine or glutamine endowed ttCK with phosphorylation activity toward uridine. These results suggested that a single amino acid residue, Tyr93, gives cytidine-limited specificity to ttCK. However, replacement of Tyr93 by Phe or Leu did not change the substrate specificity of ttCK. Therefore, we conclude that a residue at this position is essential for the recognition of uridine by UCK. In addition, thymidine phosphorylase from T. thermophilus HB8 was equally active with thymidine and uridine, which indicates that this protein is the sole enzyme metabolizing uridine in T. Thermophilus HB8. On the basis of these results, we discuss the pyrimidine-salvage pathway in T. thermophilus HB8.
A Single Amino Acid Limits the Substrate Specificity of Thermus thermophilus Uridine-Cytidine Kinase to Cytidine.,Tomoike F, Nakagawa N, Kuramitsu S, Masui R Biochemistry. 2011 May 31;50(21):4597-607. Epub 2011 May 3. PMID:21539325[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tomoike F, Nakagawa N, Kuramitsu S, Masui R. A Single Amino Acid Limits the Substrate Specificity of Thermus thermophilus Uridine-Cytidine Kinase to Cytidine. Biochemistry. 2011 May 31;50(21):4597-607. Epub 2011 May 3. PMID:21539325 doi:10.1021/bi102054n
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