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Oxidoreductase PDB id
1n2n
Jmol
Contents
Protein chains
419 a.a. *
Ligands
CYN
HEM ×2
H4B ×2
ARG ×2
Metals
_ZN ×2
Waters ×530
* Residue conservation analysis
PDB id:
1n2n
Name: Oxidoreductase
Title: Crystal structure of cyanide complex of the oxygenase domain inducible nitric oxide synthase.
Structure: Inducible nitric oxide synthase. Chain: a, b. Fragment: oxygenase domain. Synonym: nos, type ii, inducible nos. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
2.40Å     R-factor:   0.206     R-free:   0.243
Authors: R.Fedorov,D.K.Ghosh,I.Schlichting
Key ref: R.Fedorov et al. (2003). Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes. Arch Biochem Biophys, 409, 25-31. PubMed id: 12464241 DOI: 10.1016/S0003-9861(02)00555-6
Date:
23-Oct-02     Release date:   11-Feb-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P29477  (NOS2_MOUSE) -  Nitric oxide synthase, inducible
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1144 a.a.
419 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.14.13.39  - Nitric-oxide synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
L-arginine
Bound ligand (Het Group name = ARG)
matches with 91.67% similarity 		+ n NADPH
 + n H(+)
 + m O(2)
 = citrulline
 + nitric oxide
 + n NADP(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     calmodulin binding     7 terms  

 

 
    reference    
 
 
DOI no: 10.1016/S0003-9861(02)00555-6 Arch Biochem Biophys 409:25-31 (2003)
PubMed id: 12464241  
 
 
Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes.
R.Fedorov, D.K.Ghosh, I.Schlichting.
 
  ABSTRACT  
 
The crystal structure of the ternary cyanide complex of P450cam and camphor was determined to 1.8A resolution and found to be identical with the structure of the active oxygen complex [I. Schlichting et al., 2000, Science 287, 1615]. Notably, cyanide binds in a bent mode and induces the active conformation that is characterized by the presence of two water molecules and a flip of the carbonyl of the conserved Asp251. The structure of the ternary complex of cyanide, L-arginine, and the oxygenase domain of inducible nitric oxide synthase was determined to 2.4A resolution. Cyanide binds essentially linearly, interacts with L-Arg, and induces the binding of a water molecule at the active site. This water is positioned by backbone interactions, located 2.8A from the nitrogen atom of cyanide, and could provide a proton required for O-O bond scission in the hydroxylation reaction of nitric oxide synthase.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20446763 T.C.Pochapsky, S.Kazanis, and M.Dang (2010).
Conformational plasticity and structure/function relationships in cytochromes P450.
  Antioxid Redox Signal, 13, 1273-1296.  
20606257 V.S.de Serrano, M.F.Davis, J.F.Gaff, Q.Zhang, Z.Chen, E.L.D'Antonio, E.F.Bowden, R.Rose, and S.Franzen (2010).
X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: evidence for photoreductive dissociation of the iron-cyanide bond.
  Acta Crystallogr D Biol Crystallogr, 66, 770-782.
PDB codes: 3kun 3kuo
18180042 M.Freindorf, Y.Shao, J.Kong, and T.R.Furlani (2008).
Combined QM/MM calculations of active-site vibrations in binding process of P450cam to putidaredoxin.
  J Inorg Biochem, 102, 427-432.  
17598143 H.Yao, C.R.McCullough, A.D.Costache, P.K.Pullela, and D.S.Sem (2007).
Structural evidence for a functionally relevant second camphor binding site in P450cam: model for substrate entry into a P450 active site.
  Proteins, 69, 125-138.  
  17554165 M.Sugishima, K.Oda, T.Ogura, H.Sakamoto, M.Noguchi, and K.Fukuyama (2007).
Alternative cyanide-binding modes to the haem iron in haem oxygenase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 471-474.
PDB code: 2e7e
17881827 V.de Serrano, Z.Chen, M.F.Davis, and S.Franzen (2007).
X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata.
  Acta Crystallogr D Biol Crystallogr, 63, 1094-1101.
PDB codes: 2qfk 2qfn
16367758 D.Lefèvre-Groboillot, J.L.Boucher, D.Mansuy, and D.J.Stuehr (2006).
Reactivity of the heme-dioxygen complex of the inducible nitric oxide synthase in the presence of alternative substrates.
  FEBS J, 273, 180-191.  
16804678 H.Li, J.Igarashi, J.Jamal, W.Yang, and T.L.Poulos (2006).
Structural studies of constitutive nitric oxide synthases with diatomic ligands bound.
  J Biol Inorg Chem, 11, 753-768.
PDB codes: 2g6h 2g6i 2g6j 2g6k 2g6l 2g6m 2g6n 2g6o
16790441 K.Kühnel, W.Blankenfeldt, J.Terner, and I.Schlichting (2006).
Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate.
  J Biol Chem, 281, 23990-23998.
PDB codes: 2civ 2ciw 2cix 2ciy 2ciz 2cj0 2cj1 2cj2
16235218 C.Jung, F.Lendzian, V.Schünemann, M.Richter, L.H.Böttger, A.X.Trautwein, J.Contzen, M.Galander, D.K.Ghosh, and A.L.Barra (2005).
Multi-frequency EPR and Mössbauer spectroscopic studies on freeze-quenched reaction intermediates of nitric oxide synthase.
  Magn Reson Chem, 43, S84-S95.  
15066989 D.Li, D.J.Stuehr, S.R.Yeh, and D.L.Rousseau (2004).
Heme distortion modulated by ligand-protein interactions in inducible nitric-oxide synthase.
  J Biol Chem, 279, 26489-26499.  
15224385 H.Matter, and P.Kotsonis (2004).
Biology and chemistry of the inhibition of nitric oxide synthases by pteridine-derivatives as therapeutic agents.
  Med Res Rev, 24, 662-684.  
15189165 O.Pylypenko, and I.Schlichting (2004).
Structural aspects of ligand binding to and electron transfer in bacterial and fungal P450s.
  Annu Rev Biochem, 73, 991.  
15071192 R.Fedorov, R.Vasan, D.K.Ghosh, and I.Schlichting (2004).
Structures of nitric oxide synthase isoforms complexed with the inhibitor AR-R17477 suggest a rational basis for specificity and inhibitor design.
  Proc Natl Acad Sci U S A, 101, 5892-5897.
PDB codes: 1vaf 1vag
15269210 S.Nagano, T.Tosha, K.Ishimori, I.Morishima, and T.L.Poulos (2004).
Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding.
  J Biol Chem, 279, 42844-42849.
PDB codes: 1t85 1t86 1t87 1t88
12954642 R.Fedorov, E.Hartmann, D.K.Ghosh, and I.Schlichting (2003).
Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and Nomega-propyl-L-Arg for the inducible and neuronal isoforms.
  J Biol Chem, 278, 45818-45825.
PDB codes: 1qw4 1qw5 1qw6 1qwc
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.