1mc3

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[[Image:1mc3.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF RFFH==
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|PDB= 1mc3 |SIZE=350|CAPTION= <scene name='initialview01'>1mc3</scene>, resolution 2.6&Aring;
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<StructureSection load='1mc3' size='340' side='right'caption='[[1mc3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TTP:THYMIDINE-5&#39;-TRIPHOSPHATE'>TTP</scene>
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<table><tr><td colspan='2'>[[1mc3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MC3 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24] </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]] 2.6&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</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=1mc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mc3 OCA], [https://pdbe.org/1mc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mc3 RCSB], [https://www.ebi.ac.uk/pdbsum/1mc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mc3 ProSAT], [https://www.topsan.org/Proteins/BSGI/1mc3 TOPSAN]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mc3 OCA], [http://www.ebi.ac.uk/pdbsum/1mc3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mc3 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/RMLA2_ECOLI RMLA2_ECOLI] Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mc/1mc3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1mc3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The enzyme glucose-1-phosphate thymidylyltransferase (RffH), the product of the rffh gene, catalyzes one of the steps in the synthesis of enterobacterial common antigen (ECA), a cell surface glycolipid found in Gram-negative enteric bacteria. In Escherichia coli two gene products, RffH and RmlA, catalyze the same enzymatic reaction and are homologous in sequence; however, they are part of different operons and function in different pathways. We report the crystal structure of RffH bound to deoxythymidine triphosphate (dTTP), the phosphate donor, and Mg(2+), refined at 2.6 A to an R-factor of 22.3% (R(free) = 28.4%). The crystal structure of RffH shows a tetrameric enzyme best described as a dimer of dimers. Each monomer has an overall alpha/beta fold and consists of two domains, a larger nucleotide binding domain (residues 1-115, 222-291) and a smaller sugar-binding domain (116-221), with the active site located at the domain interface. The Mg(2+) ion is coordinated by two conserved aspartates and the alpha-phosphate of deoxythymidine triphosphate. Its location corresponds well to that in a structurally similar domain of N-acetylglucosamine-1-phosphate uridylyltransferase (GlmU). Analysis of the RffH, RmlA, and GlmU complexes with substrates and products provides an explanation for their different affinities for Mg(2+) and leads to a proposal for the dynamics along the reaction pathway.
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'''CRYSTAL STRUCTURE OF RFFH'''
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Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+.,Sivaraman J, Sauve V, Matte A, Cygler M J Biol Chem. 2002 Nov 15;277(46):44214-9. Epub 2002 Aug 8. PMID:12171937<ref>PMID:12171937</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1mc3" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The enzyme glucose-1-phosphate thymidylyltransferase (RffH), the product of the rffh gene, catalyzes one of the steps in the synthesis of enterobacterial common antigen (ECA), a cell surface glycolipid found in Gram-negative enteric bacteria. In Escherichia coli two gene products, RffH and RmlA, catalyze the same enzymatic reaction and are homologous in sequence; however, they are part of different operons and function in different pathways. We report the crystal structure of RffH bound to deoxythymidine triphosphate (dTTP), the phosphate donor, and Mg(2+), refined at 2.6 A to an R-factor of 22.3% (R(free) = 28.4%). The crystal structure of RffH shows a tetrameric enzyme best described as a dimer of dimers. Each monomer has an overall alpha/beta fold and consists of two domains, a larger nucleotide binding domain (residues 1-115, 222-291) and a smaller sugar-binding domain (116-221), with the active site located at the domain interface. The Mg(2+) ion is coordinated by two conserved aspartates and the alpha-phosphate of deoxythymidine triphosphate. Its location corresponds well to that in a structurally similar domain of N-acetylglucosamine-1-phosphate uridylyltransferase (GlmU). Analysis of the RffH, RmlA, and GlmU complexes with substrates and products provides an explanation for their different affinities for Mg(2+) and leads to a proposal for the dynamics along the reaction pathway.
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*[[Glucose-1-phosphate thymidylyltransferase 3D structures|Glucose-1-phosphate thymidylyltransferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1MC3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MC3 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+., Sivaraman J, Sauve V, Matte A, Cygler M, J Biol Chem. 2002 Nov 15;277(46):44214-9. Epub 2002 Aug 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12171937 12171937]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Glucose-1-phosphate thymidylyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Cygler M]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
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[[Category: Matte A]]
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[[Category: Cygler, M.]]
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[[Category: Sauve V]]
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[[Category: Matte, A.]]
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[[Category: Sivaraman J]]
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[[Category: Sauve, V.]]
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[[Category: Sivaraman, J.]]
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[[Category: bsgi]]
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[[Category: crystal structure]]
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[[Category: glucose-1-phosphate thymidylytransferase]]
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[[Category: montreal-kingston bacterial structural genomics initiative]]
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[[Category: rffh]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:14:11 2008''
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Current revision

CRYSTAL STRUCTURE OF RFFH

PDB ID 1mc3

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