1jyl

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[[Image:1jyl.gif|left|200px]]
 
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{{Structure
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==Catalytic Mechanism of CTP:phosphocholine Cytidylyltransferase from Streptococcus pneumoniae (LicC)==
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|PDB= 1jyl |SIZE=350|CAPTION= <scene name='initialview01'>1jyl</scene>, resolution 2.4&Aring;
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<StructureSection load='1jyl' size='340' side='right'caption='[[1jyl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CDC:[2-CYTIDYLATE-O&#39;-PHOSPHONYLOXYL]-ETHYL-TRIMETHYL-AMMONIUM'>CDC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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<table><tr><td colspan='2'>[[1jyl]] is a 4 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=1JYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JYL FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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|GENE= LicC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDC:[2-CYTIDYLATE-O-PHOSPHONYLOXYL]-ETHYL-TRIMETHYL-AMMONIUM'>CDC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyl OCA], [https://pdbe.org/1jyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jyl RCSB], [https://www.ebi.ac.uk/pdbsum/1jyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jyl ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1jyk|1JYK]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyl OCA], [http://www.ebi.ac.uk/pdbsum/1jyl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jyl RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/A0A0H2UQB5_STRPN A0A0H2UQB5_STRPN]
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== Evolutionary Conservation ==
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'''Catalytic Mechanism of CTP:phosphocholine Cytidylytransferase from Streptococcus pneumoniae (LicC)'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jy/1jyl_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1JYL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYL OCA].
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</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=1jyl ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11706035 11706035]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
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[[Category: Kwak, B Y.]]
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[[Category: Kwak B-Y]]
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[[Category: Park, H w.]]
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[[Category: Park H-w]]
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[[Category: Yun, M.]]
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[[Category: Yun M]]
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[[Category: 3d structure]]
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[[Category: ctp:phosphocholine cytidylyltransferase]]
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[[Category: licc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:40:48 2008''
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Current revision

Catalytic Mechanism of CTP:phosphocholine Cytidylyltransferase from Streptococcus pneumoniae (LicC)

PDB ID 1jyl

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