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Oxidoreductase PDB id
1f24
Jmol
Contents
Protein chain
399 a.a. *
Ligands
HEM-_NO
GOL
Waters ×647
* Residue conservation analysis
PDB id:
1f24
Name: Oxidoreductase
Title: Crystal structure of no complex of thr243ala mutants of cyto p450nor
Structure: Nitric oxide reductase. Chain: a. Engineered: yes. Mutation: yes
Source: Fusarium oxysporum. Organism_taxid: 5507. Expressed in: escherichia coli k12. Expression_system_taxid: 83333.
Resolution:
1.40Å     R-factor:   0.139     R-free:   0.207
Authors: H.Shimizu,S.-Y.Park
Key ref: E.Obayashi et al. (2000). Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function. J Inorg Biochem, 82, 103-111. PubMed id: 11132616 DOI: 10.1016/S0162-0134(00)00161-6
Date:
23-May-00     Release date:   23-Nov-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P23295  (NOR_FUSOX) -  Cytochrome P450 55A1
Seq:
Struc: 		403 a.a.
400 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     electron carrier activity     7 terms  

 

 
DOI no: 10.1016/S0162-0134(00)00161-6 J Inorg Biochem 82:103-111 (2000)
PubMed id: 11132616  
 
 
Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function.
E.Obayashi, H.Shimizu, S.Y.Park, H.Shoun, Y.Shiro.
 
  ABSTRACT  
 
Threonine 243 of cytochrome P450nor (fungal nitric oxide reductase) corresponds to the 'conserved' Thr in the long I helix of monooxygenase cytochrome P450s. In P450nor, the replacement of Thr243 with Asn, Ala or Val makes the enzymatic activity dramatically reduce. In order to understand the roles of Thr243 in the reduction reaction of NO by P450nor, the crystal structures of three Thr243 mutants (Thr243-->Asn, Thr243-->Val, Thr243-->Ala) of P450nor were determined at a 1.4-A resolution and at cryogenic temperature. However, the hydrogen-bonding pattern in the heme pocket of these mutants is essentially similar for that of the WT enzyme. This suggests that the determination of the structure of the NADH complex of P450nor is required, in order to evaluate the role of Thr243 in its enzymatic reaction. We attempted to crystallize the NADH complex under several conditions, but have not yet been successful.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19692330 F.Sabbadin, R.Jackson, K.Haider, G.Tampi, J.P.Turkenburg, S.Hart, N.C.Bruce, and G.Grogan (2009).
The 1.5-A structure of XplA-heme, an unusual cytochrome P450 heme domain that catalyzes reductive biotransformation of royal demolition explosive.
  J Biol Chem, 284, 28467-28475.
PDB codes: 2wiv 2wiy
17318599 A.Bonifacio, A.R.Groenhof, P.H.Keizers, C.de Graaf, J.N.Commandeur, N.P.Vermeulen, A.W.Ehlers, K.Lammertsma, C.Gooijer, and G.van der Zwan (2007).
Altered spin state equilibrium in the T309V mutant of cytochrome P450 2D6: a spectroscopic and computational study.
  J Biol Inorg Chem, 12, 645-654.  
12519772 L.M.Podust, Y.Kim, M.Arase, B.A.Neely, B.J.Beck, H.Bach, D.H.Sherman, D.C.Lamb, S.L.Kelly, and M.R.Waterman (2003).
The 1.92-A structure of Streptomyces coelicolor A3(2) CYP154C1. A new monooxygenase that functionalizes macrolide ring systems.
  J Biol Chem, 278, 12214-12221.
PDB code: 1gwi
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.