1tsx: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1tsx.jpg|left|200px]]<br /><applet load="1tsx" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1tsx, resolution 2.5&Aring;" />
-'''THYMIDYLATE SYNTHASE R179E MUTANT'''<br />
-==Overview==
+==THYMIDYLATE SYNTHASE R179E MUTANT==
-Invariant arginine 179, one of four arginines that are conserved in all, thymidylate synthases (TS) and that bind the phosphate moiety of the, substrate 2'-deoxyuridine-5'-monophosphate (dUMP), can be altered even to, a negatively charged glutamic acid with little effect on kcat. In the, mutant structures, ordered water or the other phosphate-binding arginines, compensate for the hydrogen bonds made by Arg179 in the wild-type enzyme, and there is almost no change in the conformation or binding site of dUMP., Correlation of dUMP Kds for TS R179A and TS R179K with the structures of, their binary complexes shows, that the positive charge on Arg179, contributes significantly to dUMP binding affinity. kcat/K(m) for dUMP, measures the rate of dUMP binding to TS during the ordered bi-substrate, reaction, and in the ternary complex dUMP provides a binding surface for, the cofactor. kcat/K(m) reflects the ability of the enzyme to accept a, properly oriented dUMP for catalysis and is less sensitive than is Kd to, the changes in electrostatics at the phosphate binding site.
+<StructureSection load='1tsx' size='340' side='right'caption='[[1tsx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1tsx]] 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=1TSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TSX FirstGlance]. <br>
+</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>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></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=1tsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tsx OCA], [https://pdbe.org/1tsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tsx RCSB], [https://www.ebi.ac.uk/pdbsum/1tsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tsx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TYSY_LACCA TYSY_LACCA] Provides the sole de novo source of dTMP for DNA biosynthesis.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ts/1tsx_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1tsx ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-TSX 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 UMP 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=1TSX OCA].
+*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase., Finer-Moore JS, Fauman EB, Morse RJ, Santi DV, Stroud RM, Protein Eng. 1996 Jan;9(1):69-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9053905 9053905]
+[[Category: Lacticaseibacillus casei]]
-[[Category: Lactobacillus casei]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Finer-Moore J]]
-[[Category: Thymidylate synthase]]
+[[Category: Stroud RM]]
-[[Category: Finer-Moore, J.]]
-[[Category: Stroud, R.M.]]
-[[Category: UMP]]
-[[Category: methyltransferase]]
-[[Category: nucleotide biosynthesis]]
-[[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:34:00 2007''