5d40: Difference between revisions
New page: '''Unreleased structure''' The entry 5d40 is ON HOLD Authors: Cahn, J.K.B., Dodani S.C., Arnold, F.H. Description: Crystal structure of the 5-selective H176Y mutant of Cytochrome TxtE ... |
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The | ==Crystal structure of the 5-selective H176Y mutant of Cytochrome TxtE== | ||
<StructureSection load='5d40' size='340' side='right'caption='[[5d40]], [[Resolution|resolution]] 1.51Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5d40]] is a 2 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=5D40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D40 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]] 1.51Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</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=5d40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d40 OCA], [https://pdbe.org/5d40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d40 RCSB], [https://www.ebi.ac.uk/pdbsum/5d40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d40 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C9ZDC6_STRSW C9ZDC6_STRSW] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The dynamic motions of protein structural elements, particularly flexible loops, are intimately linked with diverse aspects of enzyme catalysis. Engineering of these loop regions can alter protein stability, substrate binding and even dramatically impact enzyme function. When these flexible regions are unresolvable structurally, computational reconstruction in combination with large-scale molecular dynamics simulations can be used to guide the engineering strategy. Here we present a collaborative approach that consists of both experiment and computation and led to the discovery of a single mutation in the F/G loop of the nitrating cytochrome P450 TxtE that simultaneously controls loop dynamics and completely shifts the enzyme's regioselectivity from the C4 to the C5 position of L-tryptophan. Furthermore, we find that this loop mutation is naturally present in a subset of homologous nitrating P450s and confirm that these uncharacterized enzymes exclusively produce 5-nitro-L-tryptophan, a previously unknown biosynthetic intermediate. | |||
Discovery of a regioselectivity switch in nitrating P450s guided by molecular dynamics simulations and Markov models.,Dodani SC, Kiss G, Cahn JK, Su Y, Pande VS, Arnold FH Nat Chem. 2016 May;8(5):419-25. doi: 10.1038/nchem.2474. Epub 2016 Mar 21. PMID:27102675<ref>PMID:27102675</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5d40" style="background-color:#fffaf0;"></div> | ||
[[Category: Arnold | == References == | ||
[[Category: Dodani | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces scabiei 87 22]] | |||
[[Category: Arnold FH]] | |||
[[Category: Cahn JKB]] | |||
[[Category: Dodani SC]] | |||
Latest revision as of 11:43, 27 September 2023
Crystal structure of the 5-selective H176Y mutant of Cytochrome TxtECrystal structure of the 5-selective H176Y mutant of Cytochrome TxtE
Structural highlights
FunctionPublication Abstract from PubMedThe dynamic motions of protein structural elements, particularly flexible loops, are intimately linked with diverse aspects of enzyme catalysis. Engineering of these loop regions can alter protein stability, substrate binding and even dramatically impact enzyme function. When these flexible regions are unresolvable structurally, computational reconstruction in combination with large-scale molecular dynamics simulations can be used to guide the engineering strategy. Here we present a collaborative approach that consists of both experiment and computation and led to the discovery of a single mutation in the F/G loop of the nitrating cytochrome P450 TxtE that simultaneously controls loop dynamics and completely shifts the enzyme's regioselectivity from the C4 to the C5 position of L-tryptophan. Furthermore, we find that this loop mutation is naturally present in a subset of homologous nitrating P450s and confirm that these uncharacterized enzymes exclusively produce 5-nitro-L-tryptophan, a previously unknown biosynthetic intermediate. Discovery of a regioselectivity switch in nitrating P450s guided by molecular dynamics simulations and Markov models.,Dodani SC, Kiss G, Cahn JK, Su Y, Pande VS, Arnold FH Nat Chem. 2016 May;8(5):419-25. doi: 10.1038/nchem.2474. Epub 2016 Mar 21. PMID:27102675[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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