2qcx: Difference between revisions
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<StructureSection load='2qcx' size='340' side='right'caption='[[2qcx]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2qcx' size='340' side='right'caption='[[2qcx]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qcx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2qcx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QCX FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PF1:N-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-N-(2-HYDROXYETHYL)FORMAMIDE'>PF1</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=2qcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qcx OCA], [https://pdbe.org/2qcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qcx RCSB], [https://www.ebi.ac.uk/pdbsum/2qcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qcx ProSAT]</span></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=2qcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qcx OCA], [https://pdbe.org/2qcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qcx RCSB], [https://www.ebi.ac.uk/pdbsum/2qcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qcx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TENA_BACSU TENA_BACSU] Stimulates the production of several extracellular degradative enzymes at the transcriptional level, probably by interfering with DegS and DegU, which are required for this effect. Is not an essential protein, but affects the sporulation frequency. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus subtilis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Begley | [[Category: Begley TP]] | ||
[[Category: Ealick | [[Category: Ealick SE]] | ||
[[Category: Jenkins | [[Category: Jenkins AL]] | ||
[[Category: Zhang | [[Category: Zhang Y]] | ||
Latest revision as of 14:29, 30 August 2023
Crystal structure of Bacillus subtilis TenA Y112F mutant complexed with formyl aminomethyl pyrimidineCrystal structure of Bacillus subtilis TenA Y112F mutant complexed with formyl aminomethyl pyrimidine
Structural highlights
FunctionTENA_BACSU Stimulates the production of several extracellular degradative enzymes at the transcriptional level, probably by interfering with DegS and DegU, which are required for this effect. Is not an essential protein, but affects the sporulation frequency. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTenA catalyzes the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine and participates in the salvage of base-degraded thiamin. Here, we describe mutagenesis of the active site of TenA guided by structures of the enzyme complexed to a substrate analog and to the product. Catalytic roles for each of the active site residues are identified and a mechanism for the reaction is described. Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis.,Jenkins AL, Zhang Y, Ealick SE, Begley TP Bioorg Chem. 2008 Feb;36(1):29-32. Epub 2007 Dec 3. PMID:18054064[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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