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<StructureSection load='1tzf' size='340' side='right'caption='[[1tzf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1tzf' size='340' side='right'caption='[[1tzf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1tzf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhi_ct18 Salmonella enterica subsp. enterica serovar typhi ct18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TZF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1tzf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhi_str._CT18 Salmonella enterica subsp. enterica serovar Typhi str. CT18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TZF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C5G:[CYTIDINE-5-PHOSPHATE]-BETA-GLUCOSYL-PHOSPHORIC+ACID+ESTER'>C5G</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.1&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rfbF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=220341 Salmonella enterica subsp. enterica serovar Typhi CT18])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C5G:[CYTIDINE-5-PHOSPHATE]-BETA-GLUCOSYL-PHOSPHORIC+ACID+ESTER'>C5G</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-1-phosphate_cytidylyltransferase Glucose-1-phosphate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.33 2.7.7.33] </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=1tzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzf OCA], [https://pdbe.org/1tzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tzf RCSB], [https://www.ebi.ac.uk/pdbsum/1tzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tzf 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=1tzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzf OCA], [http://pdbe.org/1tzf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tzf RCSB], [http://www.ebi.ac.uk/pdbsum/1tzf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tzf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RFBF_SALTY RFBF_SALTY]] Involved in the biosynthesis of the tyvelose, a 3,6-dideoxyhexose found in the O-antigen of the surface lipopolysaccharides. It catalyzes the transfer of a CMP moiety from CTP to glucose 1-phosphate (By similarity).  
[https://www.uniprot.org/uniprot/RFBF_SALTI RFBF_SALTI] Involved in the biosynthesis of the tyvelose, a 3,6-dideoxyhexose found in the O-antigen of the surface lipopolysaccharides. It catalyzes the transfer of a CMP moiety from CTP to glucose 1-phosphate. This enzyme can utilize either CTP or UTP as the nucleotide donor.<ref>PMID:15634670</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1tzf ConSurf].
</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=1tzf ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dideoxysugars, which display biological activities ranging from mediating cell-cell interactions to serving as components in some antibiotics, are synthesized in various organisms via complex biochemical pathways that begin with the attachment of alpha-D-glucose 1-phosphate to either CTP or dTTP. Here we describe the three-dimensional structure of the alpha-D-glucose-1-phosphate cytidylyltransferase from Salmonella typhi, which catalyzes the first step in the production of CDP-tyvelose. For this investigation, the enzyme was crystallized in the presence of its product, CDP-glucose. In contrast to previous reports, the enzyme exists as a fully integrated hexamer with 32-point group symmetry. Each subunit displays a "bird-like" appearance with the "body" composed predominantly of a seven-stranded mixed beta-sheet and the two "wings" formed by beta-hairpin motifs. These two wings mediate subunit-subunit interactions along the 3-fold and 2-fold rotational axes, respectively. The six active sites of the hexamer are situated between the subunits related by the 2-fold rotational axes. CDP-glucose is anchored to the protein primarily by hydrogen bonds with backbone carbonyl oxygens and peptidic NH groups. The side chains of Arg111 and Asn188 from one subunit and Glu178 and Lys179 from the second subunit are also involved in hydrogen bonding with the ligand. The topology of the main core domain bears striking similarity to that observed for glucose-1-phosphate thymidylyltransferase and 4-diphosphocytidyl-2-C-methylerythritol synthetase.
Molecular structure of alpha-D-glucose-1-phosphate cytidylyltransferase from Salmonella typhi.,Koropatkin NM, Holden HM J Biol Chem. 2004 Oct 15;279(42):44023-9. Epub 2004 Aug 3. PMID:15292268<ref>PMID:15292268</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tzf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glucose-1-phosphate cytidylyltransferase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar typhi ct18]]
[[Category: Salmonella enterica subsp. enterica serovar Typhi str. CT18]]
[[Category: Holden, H M]]
[[Category: Holden HM]]
[[Category: Koropatkin, N M]]
[[Category: Koropatkin NM]]
[[Category: Mixed alpha/beta fold]]
[[Category: Nucleotidyltransferase]]
[[Category: Transferase]]

Latest revision as of 08:43, 14 February 2024

X-ray Crystal Structure of alpha-D-glucose-1-phosphate cytidylyltransferase from Salmonella typhi

1tzf, resolution 2.10Å

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