1bq2

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[[Image:1bq2.gif|left|200px]]
 
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==E. COLI THYMIDYLATE SYNTHASE MUTANT N177A==
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The line below this paragraph, containing "STRUCTURE_1bq2", creates the "Structure Box" on the page.
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<StructureSection load='1bq2' size='340' side='right'caption='[[1bq2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1bq2]] 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=1BQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BQ2 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.2&#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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_1bq2| PDB=1bq2 | SCENE= }}
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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=1bq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bq2 OCA], [https://pdbe.org/1bq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bq2 RCSB], [https://www.ebi.ac.uk/pdbsum/1bq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bq2 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/bq/1bq2_consurf.spt"</scriptWhenChecked>
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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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</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=1bq2 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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Mutation of thymidylate synthase N229(177) to alanine results in an essentially inactive enzyme, yet it leads to formation of a stable ternary complex. The kinetics of N229(177)A show that kcat for Escherichia coli is reduced by 200-fold while the Km for dUMP is increased 200-fold and the Km for folate increased by tenfold versus the wild-type enzyme. The crystal structures of N229(177)A in complex with dUMP and CB3717, and in complex with dUMP alone are determined at 2.4 A, and 2.5 A resolution. These structures identify the covalently bound ternary complex and show how N229(177)A traps an intermediate, and so becomes inactive in a later step of the reaction. Since the smaller alanine side-chain at N229(177)A does not directly sterically impair binding of ligands, the structures implicate, and place quantitative limits on the involvement of the structured water network in the active site of thymidylate synthase in both catalysis and in determining the binding affinity for dUMP (in contrast, the N229(177)V mutation in Lactobacillus casei has minimal effect on activity).
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'''E. COLI THYMIDYLATE SYNTHASE MUTANT N177A'''
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Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer.,Reyes CL, Sage CR, Rutenber EE, Nissen RM, Finer-Moore JS, Stroud RM J Mol Biol. 1998 Dec 4;284(3):699-712. PMID:9826509<ref>PMID:9826509</ref>
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==Overview==
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Mutation of thymidylate synthase N229(177) to alanine results in an essentially inactive enzyme, yet it leads to formation of a stable ternary complex. The kinetics of N229(177)A show that kcat for Escherichia coli is reduced by 200-fold while the Km for dUMP is increased 200-fold and the Km for folate increased by tenfold versus the wild-type enzyme. The crystal structures of N229(177)A in complex with dUMP and CB3717, and in complex with dUMP alone are determined at 2.4 A, and 2.5 A resolution. These structures identify the covalently bound ternary complex and show how N229(177)A traps an intermediate, and so becomes inactive in a later step of the reaction. Since the smaller alanine side-chain at N229(177)A does not directly sterically impair binding of ligands, the structures implicate, and place quantitative limits on the involvement of the structured water network in the active site of thymidylate synthase in both catalysis and in determining the binding affinity for dUMP (in contrast, the N229(177)V mutation in Lactobacillus casei has minimal effect on activity).
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1BQ2 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=1BQ2 OCA].
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</div>
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<div class="pdbe-citations 1bq2" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer., Reyes CL, Sage CR, Rutenber EE, Nissen RM, Finer-Moore JS, Stroud RM, J Mol Biol. 1998 Dec 4;284(3):699-712. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9826509 9826509]
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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>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Thymidylate synthase]]
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[[Category: Finer-Moore JS]]
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[[Category: Finer-Moore, J S.]]
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[[Category: Reyes CL]]
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[[Category: Reyes, C L.]]
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[[Category: Rutenber EE]]
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[[Category: Rutenber, E E.]]
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[[Category: Sage CR]]
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[[Category: Sage, C R.]]
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[[Category: Stroud RM]]
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[[Category: Stroud, R M.]]
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[[Category: Methyltransferase]]
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[[Category: Substrate module]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:49:00 2008''
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Current revision

E. COLI THYMIDYLATE SYNTHASE MUTANT N177A

PDB ID 1bq2

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