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1n1d

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[[Image:1n1d.gif|left|200px]]
 
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{{Structure
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==Glycerol-3-phosphate cytidylyltransferase complexed with CDP-glycerol==
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|PDB= 1n1d |SIZE=350|CAPTION= <scene name='initialview01'>1n1d</scene>, resolution 2.&Aring;
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<StructureSection load='1n1d' size='340' side='right'caption='[[1n1d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=C2G:[CYTIDINE-5&#39;-PHOSPHATE]+GLYCERYLPHOSPHORIC+ACID+ESTER'>C2G</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1n1d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N1D FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerol-3-phosphate_cytidylyltransferase Glycerol-3-phosphate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.39 2.7.7.39] </span>
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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&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2G:[CYTIDINE-5-PHOSPHATE]+GLYCERYLPHOSPHORIC+ACID+ESTER'>C2G</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1n1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1d OCA], [https://pdbe.org/1n1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n1d RCSB], [https://www.ebi.ac.uk/pdbsum/1n1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n1d ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1coz|1COZ]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1d OCA], [http://www.ebi.ac.uk/pdbsum/1n1d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n1d RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/TAGD_BACSU TAGD_BACSU] Provides activated glycerol phosphate for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF.
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== Evolutionary Conservation ==
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'''Glycerol-3-phosphate cytidylyltransferase complexed with CDP-glycerol'''
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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/n1/1n1d_consurf.spt"</scriptWhenChecked>
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The bacterial enzyme, glycerol-3-phosphate cytidylyltransferase (GCT), is a model for mammalian cytidylyltransferases and is a member of a large superfamily of nucleotidyltransferases. Dimeric GCT from Bacillus subtilis displays unusual negative cooperativity in substrate binding and appears to form products only when both active sites are occupied by substrates. Here we describe a complex of GCT with the product, CDP-glycerol, in a crystal structure in which bound sulfate serves as a partial mimic of the second product, pyrophosphate. Binding of sulfate to form a pseudo-ternary complex is observed in three of the four chains constituting the asymmetric unit and is accompanied by a backbone rearrangement at Asp11 and ordering of the C-terminal helix. Comparison with the CTP complex of GCT, determined previously, reveals that in the product complex the active site closes around the glycerol phosphate moiety with a concerted motion of the segment 37-47 that includes helix B. This rearrangement allows lysines 44 and 46 to interact with the glycerol and cytosine phosphates of CDP-glycerol. Binding of CDP-glycerol also induces smaller movements of residues 92-100. Roles of lysines 44 and 46 in catalysis have been confirmed by mutagenesis of these residues to alanine, which decreases Vmax(app) and has profound effects on the Km(app) for glycerol-3-phosphate.
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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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1N1D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1D 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=1n1d ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis., Pattridge KA, Weber CH, Friesen JA, Sanker S, Kent C, Ludwig ML, J Biol Chem. 2003 Dec 19;278(51):51863-71. Epub 2003 Sep 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14506262 14506262]
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Glycerol-3-phosphate cytidylyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Friesen JA]]
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[[Category: Friesen, J A.]]
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[[Category: Kent C]]
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[[Category: Kent, C.]]
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[[Category: Ludwig ML]]
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[[Category: Ludwig, M L.]]
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[[Category: Pattridge KA]]
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[[Category: Pattridge, K A.]]
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[[Category: Sankar S]]
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[[Category: Sankar, S.]]
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[[Category: Weber CH]]
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[[Category: Weber, C H.]]
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[[Category: alpha/beta fold]]
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[[Category: cdp-glycerol]]
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[[Category: cytidylyltransferase]]
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[[Category: negative cooperativity]]
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[[Category: nucleotidyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:23:59 2008''
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Current revision

Glycerol-3-phosphate cytidylyltransferase complexed with CDP-glycerol

PDB ID 1n1d

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