4up2
From Proteopedia
(Difference between revisions)
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4up1|4up1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4up1|4up1]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophanase Tryptophanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.1 4.1.99.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophanase Tryptophanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.1 4.1.99.1] </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=4up2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4up2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4up2 RCSB], [http://www.ebi.ac.uk/pdbsum/4up2 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=4up2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4up2 OCA], [http://pdbe.org/4up2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4up2 RCSB], [http://www.ebi.ac.uk/pdbsum/4up2 PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tryptophanase is a bacterial enzyme involved in the degradation of tryptophan to indole, pyruvate and ammonia, which are compounds that are essential for bacterial survival. Tryptophanase is often overexpressed in stressed cultures. Large amounts of endogenous tryptophanase were purified from Escherichia coli BL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space group P6522 in the apo form without pyridoxal 5'-phosphate bound in the active site. | ||
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| + | Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture.,Rety S, Deschamps P, Leulliot N Acta Crystallogr F Struct Biol Commun. 2015 Nov 1;71(Pt 11):1378-83. doi:, 10.1107/S2053230X15017549. Epub 2015 Oct 23. PMID:26527264<ref>PMID:26527264</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4up2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 21:00, 30 November 2015
Crystal structure of Escherichia coli tryptophanase purified from alkaline stressed bacterial culture.
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