2ftn

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(New page: 200px<br /><applet load="2ftn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ftn, resolution 1.60&Aring;" /> '''E. coli thymidylate ...)
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[[Image:2ftn.gif|left|200px]]<br /><applet load="2ftn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ftn, resolution 1.60&Aring;" />
 
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'''E. coli thymidylate synthase Y94F mutant'''<br />
 
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==Overview==
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==E. coli thymidylate synthase Y94F mutant==
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Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction, of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP), substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic, activity. The structure of the Y94F mutant has been determined in the, native state and as a ternary complex with thymidine 5'-monophosphate, (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural, changes ascribable to the mutation other than loss of a water molecule, hydrogen bonded to the tyrosine OH, which is consistent with a catalytic, role for the phenolic OH.
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<StructureSection load='2ftn' size='340' side='right'caption='[[2ftn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ftn]] is a 1 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=2FTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FTN FirstGlance]. <br>
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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]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXM:N-CARBOXYMETHIONINE'>CXM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=2ftn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ftn OCA], [https://pdbe.org/2ftn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ftn RCSB], [https://www.ebi.ac.uk/pdbsum/2ftn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ftn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TYSY_ECOLI TYSY_ECOLI] Provides the sole de novo source of dTMP for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation.
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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/ft/2ftn_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=2ftn 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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Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.
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==About this Structure==
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Structure of the Y94F mutant of Escherichia coli thymidylate synthase.,Roberts SA, Hyatt DC, Honts JE, Changchien L, Maley GF, Maley F, Montfort WR Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):840-3. Epub 2006 Aug 18. PMID:16946460<ref>PMID:16946460</ref>
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2FTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FTN OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of the Y94F mutant of Escherichia coli thymidylate synthase., Roberts SA, Hyatt DC, Honts JE, Changchien L, Maley GF, Maley F, Montfort WR, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):840-3. Epub 2006 Aug 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16946460 16946460]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2ftn" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Thymidylate synthase]]
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[[Category: Montfort, W.R.]]
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[[Category: Roberts, S.A.]]
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[[Category: SO4]]
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[[Category: methyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:45:51 2007''
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==See Also==
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*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Montfort WR]]
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[[Category: Roberts SA]]

Current revision

E. coli thymidylate synthase Y94F mutant

PDB ID 2ftn

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