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| | <StructureSection load='1jyk' size='340' side='right'caption='[[1jyk]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='1jyk' size='340' side='right'caption='[[1jyk]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1jyk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JYK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1jyk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JYK FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jyl|1jyl]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LicC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</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=1jyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyk OCA], [https://pdbe.org/1jyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jyk RCSB], [https://www.ebi.ac.uk/pdbsum/1jyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jyk ProSAT]</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=1jyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyk OCA], [http://pdbe.org/1jyk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jyk RCSB], [http://www.ebi.ac.uk/pdbsum/1jyk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jyk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LICC_STRR6 LICC_STRR6] Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis (PubMed:8837483). Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho) (PubMed:11466299, PubMed:11706035, PubMed:11786295, PubMed:31420548, PubMed:8837483). Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency (PubMed:11466299, PubMed:31420548). Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP (PubMed:11466299, PubMed:11786295).<ref>PMID:11466299</ref> <ref>PMID:11706035</ref> <ref>PMID:11786295</ref> <ref>PMID:31420548</ref> <ref>PMID:8837483</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jy/1jyk_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jy/1jyk_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kwak, B Y]] | + | [[Category: Streptococcus pneumoniae]] |
| - | [[Category: Park, H w]] | + | [[Category: Kwak B-Y]] |
| - | [[Category: Yun, M]] | + | [[Category: Park H-w]] |
| - | [[Category: 3d structure]]
| + | [[Category: Yun M]] |
| - | [[Category: Ctp:phosphocholine cytidylyltransferase]]
| + | |
| - | [[Category: Licc]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
LICC_STRR6 Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis (PubMed:8837483). Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho) (PubMed:11466299, PubMed:11706035, PubMed:11786295, PubMed:31420548, PubMed:8837483). Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency (PubMed:11466299, PubMed:31420548). Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP (PubMed:11466299, PubMed:11786295).[1] [2] [3] [4] [5]
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
Pneumococcal LicC is a member of the nucleoside triphosphate transferase superfamily and catalyzes the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. The structures of apo-LicC and the LicC-CDP-choline-Mg(2+) ternary complex were determined, and the comparison of these structures reveals a significant conformational change driven by the multivalent coordination of Mg(2+). The key event is breaking the Glu(216)-Arg(129) salt bridge, which triggers the coalescence of four individual beta-strands into two extended beta-sheets. These movements reorient the side chains of Trp(136) and Tyr(190) for the optimal binding and alignment of the phosphocholine moiety. Consistent with these conformational changes, LicC operates via a compulsory ordered kinetic mechanism. The structures explain the substrate specificity of LicC for CTP and phosphocholine and implicate a direct role for Mg(2+) in aligning phosphocholine for in-line nucleophilic attack and stabilizing the negative charge that develops in the pentacoordinate transition state. These results provide a structural basis for assigning a specific role for magnesium in the catalytic mechanism of pneumococcal LicC.
Structure and mechanism of CTP:phosphocholine cytidylyltransferase (LicC) from Streptococcus pneumoniae.,Kwak BY, Zhang YM, Yun M, Heath RJ, Rock CO, Jackowski S, Park HW J Biol Chem. 2002 Feb 8;277(6):4343-50. Epub 2001 Nov 12. PMID:11706035[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rock CO, Heath RJ, Park HW, Jackowski S. The licC gene of Streptococcus pneumoniae encodes a CTP:phosphocholine cytidylyltransferase. J Bacteriol. 2001 Aug;183(16):4927-31. PMID:11466299 doi:10.1128/JB.183.16.4927-4931.2001
- ↑ Kwak BY, Zhang YM, Yun M, Heath RJ, Rock CO, Jackowski S, Park HW. Structure and mechanism of CTP:phosphocholine cytidylyltransferase (LicC) from Streptococcus pneumoniae. J Biol Chem. 2002 Feb 8;277(6):4343-50. Epub 2001 Nov 12. PMID:11706035 doi:http://dx.doi.org/10.1074/jbc.M109163200
- ↑ Campbell HA, Kent C. The CTP:phosphocholine cytidylyltransferase encoded by the licC gene of Streptococcus pneumoniae: cloning, expression, purification, and characterization. Biochim Biophys Acta. 2001 Dec 30;1534(2-3):85-95. PMID:11786295 doi:10.1016/s1388-1981(01)00174-3
- ↑ Rice K, Batul K, Whiteside J, Kelso J, Papinski M, Schmidt E, Pratasouskaya A, Wang D, Sullivan R, Bartlett C, Weadge JT, Van der Kamp MW, Moreno-Hagelsieb G, Suits MD, Horsman GP. The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis. Nat Commun. 2019 Aug 16;10(1):3698. doi: 10.1038/s41467-019-11627-6. PMID:31420548 doi:http://dx.doi.org/10.1038/s41467-019-11627-6
- ↑ Whiting GC, Gillespie SH. Investigation of a choline phosphate synthesis pathway in Streptococcus pneumoniae: evidence for choline phosphate cytidylyltransferase activity. FEMS Microbiol Lett. 1996 Oct 1;143(2-3):279-84. PMID:8837483 doi:10.1111/j.1574-6968.1996.tb08493.x
- ↑ Kwak BY, Zhang YM, Yun M, Heath RJ, Rock CO, Jackowski S, Park HW. Structure and mechanism of CTP:phosphocholine cytidylyltransferase (LicC) from Streptococcus pneumoniae. J Biol Chem. 2002 Feb 8;277(6):4343-50. Epub 2001 Nov 12. PMID:11706035 doi:http://dx.doi.org/10.1074/jbc.M109163200
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