4tpn: Difference between revisions
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==High-resolution structure of TxtE in the absence of substrate== | |||
<StructureSection load='4tpn' size='340' side='right'caption='[[4tpn]], [[Resolution|resolution]] 1.18Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4tpn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_scabiei_87.22 Streptomyces scabiei 87.22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TPN 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]] 1.18Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene>, <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=4tpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tpn OCA], [https://pdbe.org/4tpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tpn RCSB], [https://www.ebi.ac.uk/pdbsum/4tpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tpn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C9ZDC6_STRSW C9ZDC6_STRSW] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4tpn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces scabiei 87 22]] | |||
[[Category: Arnold FH]] | |||
[[Category: Brinkmann-Chen S]] | |||
[[Category: Cahn JKB]] | |||
[[Category: Dodani SC]] | |||
[[Category: Heinsich T]] | |||
[[Category: McIntosh JA]] | |||
