2qcx: Difference between revisions
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==Crystal structure of Bacillus subtilis TenA Y112F mutant complexed with formyl aminomethyl pyrimidine== | ==Crystal structure of Bacillus subtilis TenA Y112F mutant complexed with formyl aminomethyl pyrimidine== | ||
<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=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tenA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tenA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminopyrimidine_aminohydrolase Aminopyrimidine aminohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.2 3.5.99.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminopyrimidine_aminohydrolase Aminopyrimidine aminohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.2 3.5.99.2] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qcx OCA], [http://pdbe.org/2qcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qcx RCSB], [http://www.ebi.ac.uk/pdbsum/2qcx PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qcx OCA], [http://pdbe.org/2qcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qcx RCSB], [http://www.ebi.ac.uk/pdbsum/2qcx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qcx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2qcx" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2qcx" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:43, 18 October 2017
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
Function[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 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. References
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