2tpt: Difference between revisions
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==STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE== | |||
<StructureSection load='2tpt' size='340' side='right'caption='[[2tpt]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2tpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TPT 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]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2tpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpt OCA], [https://pdbe.org/2tpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tpt RCSB], [https://www.ebi.ac.uk/pdbsum/2tpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tpt ProSAT]</span></td></tr> | ||
[[2tpt]] is a 1 chain structure with sequence from [ | </table> | ||
== Function == | |||
== | [https://www.uniprot.org/uniprot/TYPH_ECOLI TYPH_ECOLI] The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | ||
< | == Evolutionary Conservation == | ||
[[ | [[Image:Consurf_key_small.gif|200px|right]] | ||
[[ | Check<jmol> | ||
[[ | <jmolCheckbox> | ||
[[Category: | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tp/2tpt_consurf.spt"</scriptWhenChecked> | ||
[[Category: | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
[[Category: | <text>to colour the structure by Evolutionary Conservation</text> | ||
[[Category: | </jmolCheckbox> | ||
[[Category: | </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=2tpt ConSurf]. | ||
[[Category: | <div style="clear:both"></div> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Cook WJ]] | |||
[[Category: Ealick SE]] | |||
[[Category: Jasanoff A]] | |||
[[Category: Pugmire MJ]] | |||
[[Category: Walter MR]] | |||
Latest revision as of 09:24, 21 February 2024
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
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