View source for 7q0o


==E. coli NfsA==
<StructureSection load='7q0o' size='340' side='right'caption='[[7q0o]], [[Resolution|resolution]] 0.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7q0o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q0O 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]] 0.96&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=7q0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q0o OCA], [https://pdbe.org/7q0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q0o RCSB], [https://www.ebi.ac.uk/pdbsum/7q0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q0o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NFSA_ECOLI NFSA_ECOLI] Reduction of nitroaromatic compounds using NADH. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major component of the oxygen-insensitive nitroreductase activity in E.coli.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nitroreductases activate nitroaromatic antibiotics and cancer prodrugs to cytotoxic hydroxylamines and reduce quinones to quinols. Using steady-state and stopped-flow kinetics we show that the E. coli nitroreductase NfsA is 20-50 fold more active with NADPH than with NADH and that product release may be rate-limiting. The crystal structure of NfsA with NADP(+) shows that a mobile loop forms a phosphate-binding pocket. The nicotinamide ring and nicotinamide ribose are mobile, as confirmed in molecular dynamics (MD) simulations. We present a model of NADPH bound to NfsA. Only one NADP(+) is seen bound to the NfsA dimers, and MD simulations show that binding of a second NADP(H) cofactor is unfavourable, suggesting that NfsA and other members of this protein superfamily may have a half-of-sites mechanism.

The 3D-structure, kinetics and dynamics of the E. coli nitroreductase NfsA with NADP(+) provide glimpses of its catalytic mechanism.,White SA, Christofferson AJ, Grainger AI, Day MA, Jarrom D, Graziano AE, Searle PF, Hyde EI FEBS Lett. 2022 Jun 1. doi: 10.1002/1873-3468.14413. PMID:35648111<ref>PMID:35648111</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7q0o" style="background-color:#fffaf0;"></div>

==See Also==
*[[Nitroreductase 3D structures|Nitroreductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Day MA]]
[[Category: Grainger A]]
[[Category: Graziano A]]
[[Category: Hyde EI]]
[[Category: Jarrom D]]
[[Category: Parr R]]
[[Category: Searle PF]]
[[Category: White SA]]