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TitleA Site-Saturated Mutagenesis Study of Pentaerythritol Tetranitrate Reductase Reveals that Residues 181 and 184 Influence Ligand Binding, Stereochemistry and Reactivity.
Journal, issue, pagesChembiochem, Vol. 12, Page 738-749, Year 2011
Publish dateOct 12, 2010 (structure data deposition date)
AuthorsToogood, H.S. / Fryszkowska, A. / Hulley, M. / Sakuma, M. / Mansell, D. / Stephens, G.M. / Gardiner, J.M. / Scrutton, N.S.
External linksChembiochem / PubMed:21374779
MethodsX-ray diffraction
Resolution1.2 - 2.2 Å
Structure data

PDB-3p74:
H181N mutant of pentaerythritol tetranitrate reductase containing a C-terminal His8-tag
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-3p7y:
Pentaerythritol tetranitrate reductase co-crystal structure with bound (E)-1-(2'-hydroxyphenyl)-2-nitroethene
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-3p80:
Pentaerythritol tetranitrate reductase co-crystal structure containing bound (E)-1-(3'-hydroxyphenyl)-2-nitroethene
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-3p81:
Pentaerythritol tetranitrate reductase co-crystal structure containing a bound (E)-1-(4'-hydroxyphenyl)-2-nitroethene molecule
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-3p82:
H184N mutant of pentaerythritol tetranitrate reductase containing bound acetate ion
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-HOH:
WATER

ChemComp-P7Y:
2-[(E)-2-nitroethenyl]phenol

ChemComp-P80:
3-[(E)-2-nitroethenyl]phenol

ChemComp-P81:
4-[(E)-2-nitroethenyl]phenol

ChemComp-ACT:
ACETATE ION

Source
  • enterobacter cloacae (bacteria)
KeywordsOXIDOREDUCTASE / old yellow enzyme family / alpha/beta barrel / alpha / beta barrel

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