3x21

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(Difference between revisions)

Revision as of 17:26, 9 March 2017

Crystal structure of Escherichia coli nitroreductase NfsB mutant T41L/N71S/F124W

Structural highlights

3x21 is a 10 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1ds7, 3x22
Activity:	6,7-dihydropteridine reductase, with EC number 1.5.1.34
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NFNB_ECOLI] Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.^[1]

Publication Abstract from PubMed

Nitroreductases have great potential for the highly efficient reduction of aryl nitro compounds to arylhydroxylamines. However, regioselective reduction of the desired nitro group in polynitroarenes is still a challenge. Here, we describe the structure-based engineering of Escherichia coli nitroreductase NfsB to alter its regioselectivity, in order to achieve reduction of a target nitro group. When 2,4-dinitrotoluene was used as the substrate, the wild-type enzyme regioselectively reduced the 4-NO2 group, but the T41L/N71S/F124W mutant primarily reduced the 2-NO2 group, without loss of activity. The crystal structure of T41L/N71S/F124W and docking experiments indicated that the regioselectivity change (from 4-NO2 to 2-NO2 ) might result from the increased hydrophobicity of residues 41 and 124 (proximal to FMN) and conformational changes in residues 70 and 124.

Altering the regioselectivity of a nitroreductase in the synthesis of arylhydroxylamines by structure-based engineering.,Bai J, Zhou Y, Chen Q, Yang Q, Yang J Chembiochem. 2015 May 26;16(8):1219-25. doi: 10.1002/cbic.201500070. Epub 2015, Apr 27. PMID:25917861^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Race PR, Lovering AL, Green RM, Ossor A, White SA, Searle PF, Wrighton CJ, Hyde EI. Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme. J Biol Chem. 2005 Apr 8;280(14):13256-64. Epub 2005 Jan 31. PMID:15684426 doi:http://dx.doi.org/10.1074/jbc.M409652200
↑ Bai J, Zhou Y, Chen Q, Yang Q, Yang J. Altering the regioselectivity of a nitroreductase in the synthesis of arylhydroxylamines by structure-based engineering. Chembiochem. 2015 May 26;16(8):1219-25. doi: 10.1002/cbic.201500070. Epub 2015, Apr 27. PMID:25917861 doi:http://dx.doi.org/10.1002/cbic.201500070

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3x21"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Escherichia coli nitroreductase NfsB mutant T41L/N71S/F124W==
 <StructureSection load='3x21' size='340' side='right' caption='[[3x21]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ds7|1ds7]], [[3x22|3x22]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6,7-dihydropteridine_reductase 6,7-dihydropteridine reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.34 1.5.1.34] </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=3x21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x21 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3x21 RCSB], [http://www.ebi.ac.uk/pdbsum/3x21 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=3x21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x21 OCA], [http://pdbe.org/3x21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3x21 RCSB], [http://www.ebi.ac.uk/pdbsum/3x21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3x21 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3x21" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3x21

From Proteopedia

Revision as of 17:26, 9 March 2017

Crystal structure of Escherichia coli nitroreductase NfsB mutant T41L/N71S/F124W

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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