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4tpn
From Proteopedia
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tpn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tpn RCSB], [http://www.ebi.ac.uk/pdbsum/4tpn PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tpn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tpn RCSB], [http://www.ebi.ac.uk/pdbsum/4tpn PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A novel cytochrome P450 enzyme, TxtE, was recently shown to catalyze the direct aromatic nitration of L-tryptophan. This unique chemistry inspired us to ask whether TxtE could serve as a platform for engineering new nitration biocatalysts to replace current harsh synthetic methods. As a first step toward this goal, and to better understand the wild-type enzyme, we obtained high-resolution structures of TxtE in its substrate-free and substrate-bound forms. We also screened a library of substrate analogues for spectroscopic indicators of binding and for production of nitrated products. From these results, we found that the wild-type enzyme accepts moderate decoration of the indole ring, but the amino acid moiety is crucial for binding and correct positioning of the substrate and therefore less amenable to modification. A nitrogen atom is essential for catalysis, and a carbonyl must be present to recruit the alphaB'1 helix of the protein to seal the binding pocket. | ||
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| + | Structural, Functional, and Spectroscopic Characterization of the Substrate Scope of the Novel Nitrating Cytochrome P450 TxtE.,Dodani SC, Cahn JK, Heinisch T, Brinkmann-Chen S, McIntosh JA, Arnold FH Chembiochem. 2014 Sep 2. doi: 10.1002/cbic.201402241. PMID:25182183<ref>PMID:25182183</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:20, 24 September 2014
High-resolution structure of TxtE in the absence of substrate
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