1vzd

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(New page: 200px<br /><applet load="1vzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vzd, resolution 2.5&Aring;" /> '''L. CASEI THYMIDYLATE ...)
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[[Image:1vzd.jpg|left|200px]]<br /><applet load="1vzd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1vzd, resolution 2.5&Aring;" />
 
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'''L. CASEI THYMIDYLATE SYNTHASE MUTANT E60Q TERNARY COMPLEX WITH FDUMP AND CB3717'''<br />
 
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==Overview==
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==L. CASEI THYMIDYLATE SYNTHASE MUTANT E60Q TERNARY COMPLEX WITH FDUMP AND CB3717==
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Three steps along the pathway of binding, orientation of substrates and, release of products are revealed by X-ray crystallographic structures of, ternary complexes of the wild-type Lactobacillus casei thymidylate, synthase enzyme. Each complex was formed by diffusion of either the, cofactor 5,10-methylene-5,6,7,8-tetrahydrofolate or the folate analog, 10-propargyl-5,8-dideazafolate into binary co-crystals of thymidylate, synthase with 2'-deoxyuridine-5'-monophosphate. A two-substrate/enzyme, complex is formed where the substrates remain unaltered. The imidazolidine, ring is unopened and the pterin of the, 5,10-methylene-5,6,7,8-tetrahydrofolate cofactor binds at an unproductive, "alternate" site. We propose that the presence of the pterin at this site, may represent an initial interaction with the enzyme that precedes all, catalytic events. The structure of the 2'-deoxyuridine-5'-monophosphate, and 10-propargyl-5,8-dideazafolate folate analog complex identifies both, ligands in orientations favorable for the initiation of catalysis and, resembles the productive complex. A product complex where the ligands have, been converted into products of the thymidylate synthase reaction within, the crystal, 2'-deoxythymidine-5'-monophosphate and 7,8-dihydrofolate, shows how ligands are situated within the enzyme after catalysis and on, the way to product release.
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<StructureSection load='1vzd' size='340' side='right'caption='[[1vzd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1vzd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lacticaseibacillus_casei Lacticaseibacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZD 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]] 2.5&#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=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=UFP:5-FLUORO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>UFP</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=1vzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzd OCA], [https://pdbe.org/1vzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzd RCSB], [https://www.ebi.ac.uk/pdbsum/1vzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TYSY_LACCA TYSY_LACCA] Provides the sole de novo source of dTMP for DNA biosynthesis.
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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/vz/1vzd_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=1vzd ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1VZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei] with UFP and CB3 as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1VZD OCA].
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*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Entropy in bi-substrate enzymes: proposed role of an alternate site in chaperoning substrate into, and products out of, thymidylate synthase., Birdsall DL, Finer-Moore J, Stroud RM, J Mol Biol. 1996 Jan 26;255(3):522-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8568895 8568895]
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[[Category: Lacticaseibacillus casei]]
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[[Category: Lactobacillus casei]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Birdsall DL]]
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[[Category: Thymidylate synthase]]
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[[Category: Finer-Moore J]]
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[[Category: Birdsall, D.L.]]
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[[Category: Stroud RM]]
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[[Category: Finer-Moore, J.]]
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[[Category: Stroud, R.M.]]
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[[Category: CB3]]
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[[Category: UFP]]
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[[Category: methyltransferase]]
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[[Category: nucleotide synthase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:10:46 2007''
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Current revision

L. CASEI THYMIDYLATE SYNTHASE MUTANT E60Q TERNARY COMPLEX WITH FDUMP AND CB3717

PDB ID 1vzd

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