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| | <StructureSection load='2vbs' size='340' side='right'caption='[[2vbs]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='2vbs' size='340' side='right'caption='[[2vbs]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vbs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VBS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vbs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VBS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2p3m|2p3m]], [[2vbt|2vbt]], [[2vbv|2vbv]], [[2vbu|2vbu]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/CTP-dependent_riboflavin_kinase CTP-dependent riboflavin kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.161 2.7.1.161] </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=2vbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vbs OCA], [https://pdbe.org/2vbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vbs RCSB], [https://www.ebi.ac.uk/pdbsum/2vbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vbs 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=2vbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vbs OCA], [https://pdbe.org/2vbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vbs RCSB], [https://www.ebi.ac.uk/pdbsum/2vbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vbs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RIFK_METJA RIFK_METJA]] Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN). Can also utilize UTP as the phosphate donor, although less efficiently, and it is unclear if ATP and GTP can also serve as substrates (PubMed:18245297) or not (PubMed:18073108).<ref>PMID:18073108</ref> <ref>PMID:18245297</ref>
| + | [https://www.uniprot.org/uniprot/RIFK_METJA RIFK_METJA] Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN). Can also utilize UTP as the phosphate donor, although less efficiently, and it is unclear if ATP and GTP can also serve as substrates (PubMed:18245297) or not (PubMed:18073108).<ref>PMID:18073108</ref> <ref>PMID:18245297</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43067]] | |
| - | [[Category: CTP-dependent riboflavin kinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ammelburg, M]] | + | [[Category: Methanocaldococcus jannaschii]] |
| - | [[Category: Djuranovic, S]] | + | [[Category: Ammelburg M]] |
| - | [[Category: Hartmann, M D]] | + | [[Category: Djuranovic S]] |
| - | [[Category: Lupas, A N]] | + | [[Category: Hartmann MD]] |
| - | [[Category: Martin, J]] | + | [[Category: Lupas AN]] |
| - | [[Category: Zeth, K]] | + | [[Category: Martin J]] |
| - | [[Category: Cradle-loop barrel]]
| + | [[Category: Zeth K]] |
| - | [[Category: Ctp-dependent kinase]]
| + | |
| - | [[Category: Fmn]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
RIFK_METJA Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN). Can also utilize UTP as the phosphate donor, although less efficiently, and it is unclear if ATP and GTP can also serve as substrates (PubMed:18245297) or not (PubMed:18073108).[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
Proteins of the cradle-loop barrel metafold are formed by duplication of a conserved betaalphabeta-element, suggesting a common evolutionary origin from an ancestral group of nucleic acid-binding proteins. The basal fold within this metafold, the RIFT barrel, is also found in a wide range of enzymes, whose homologous relationship with the nucleic acid-binding group is unclear. We have characterized a protein family that is intermediate in sequence and structure between the basal group of cradle-loop barrels and one family of RIFT-barrel enzymes, the riboflavin kinases. We report the structure, substrate-binding mode, and catalytic activity for one of these proteins, Methanocaldococcus jannaschii Mj0056, which is an archaeal riboflavin kinase. Mj0056 is unusual in utilizing CTP rather than ATP as the donor nucleotide, and sequence conservation in the relevant residues suggests that this is a general feature of archaeal riboflavin kinases.
A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels.,Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M Structure. 2007 Dec;15(12):1577-90. PMID:18073108[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M. A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels. Structure. 2007 Dec;15(12):1577-90. PMID:18073108 doi:10.1016/j.str.2007.09.027
- ↑ Mashhadi Z, Zhang H, Xu H, White RH. Identification and characterization of an archaeon-specific riboflavin kinase. J Bacteriol. 2008 Apr;190(7):2615-8. doi: 10.1128/JB.01900-07. Epub 2008 Feb 1. PMID:18245297 doi:http://dx.doi.org/10.1128/JB.01900-07
- ↑ Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M. A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels. Structure. 2007 Dec;15(12):1577-90. PMID:18073108 doi:10.1016/j.str.2007.09.027
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