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PDBsum entry 1foo
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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
1foo

 

 

 

 

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Contents
Protein chains
416 a.a. *
Ligands
CAC ×2
ACT ×2
HEM-_NO ×2
ARG ×2
GOL ×4
Metals
_ZN
Waters ×513
* Residue conservation analysis
PDB id:
1foo
Name: Oxidoreductase
Title: Bovine endothelial nitric oxide synthase heme domain complexed with l- arg and no(h4b-free)
Structure: Nitric-oxide synthase. Chain: a, b. Synonym: endothelial ec-nos, nos type iii, nosiii, endothelial nos, enos, constitutive nos, cnos. Engineered: yes. Other_details: cacodylate (residue cac) binds to sg cys 384 of both chains
Source: Bos taurus. Cattle. Organism_taxid: 9913. Cell: endothelial cells. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.223     R-free:   0.253
Authors: C.S.Raman,H.Li,P.Martasek,B.S.S.Masters,T.L.Poulos
Key ref:
H.Li et al. (2001). Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors. Biochemistry, 40, 5399-5406. PubMed id: 11331003 DOI: 10.1021/bi002658v
Date:
28-Aug-00     Release date:   20-Jul-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P29473  (NOS3_BOVIN) -  Nitric oxide synthase 3 from Bos taurus
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1205 a.a.
417 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.14.13.39  - nitric-oxide synthase (NADPH).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 L-arginine + 3 NADPH + 4 O2 + H+ = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
2 × L-arginine
 +
3 × NADPH
Bound ligand (Het Group name = ARG)
corresponds exactly 		+ 4 × O2
 + H(+)
 = 2 × L-citrulline
 + 2 × nitric oxide
 + 3 × NADP(+)
 + 4 × H2O
Bound ligand (Het Group name = NO)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1021/bi002658v Biochemistry 40:5399-5406 (2001)
PubMed id: 11331003  
 
 
Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors.
H.Li, C.S.Raman, P.Martásek, B.S.Masters, T.L.Poulos.
 
  ABSTRACT  
 
The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N(5)-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19841256 B.A.Patel, M.Moreau, J.Widom, H.Chen, L.Yin, Y.Hua, and B.R.Crane (2009).
Endogenous nitric oxide regulates the recovery of the radiation-resistant bacterium Deinococcus radiodurans from exposure to UV light.
  Proc Natl Acad Sci U S A, 106, 18183-18188.  
19154146 R.B.Silverman (2009).
Design of selective neuronal nitric oxide synthase inhibitors for the prevention and treatment of neurodegenerative diseases.
  Acc Chem Res, 42, 439-451.  
19663506 Y.Wang, A.F.Monzingo, S.Hu, T.H.Schaller, J.D.Robertus, and W.Fast (2009).
Developing dual and specific inhibitors of dimethylarginine dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted polypharmacology to control nitric oxide.
  Biochemistry, 48, 8624-8635.
PDB codes: 3i2e 3i4a
18815130 J.Tejero, A.Biswas, Z.Q.Wang, R.C.Page, M.M.Haque, C.Hemann, J.L.Zweier, S.Misra, and D.J.Stuehr (2008).
Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase.
  J Biol Chem, 283, 33498-33507.
PDB code: 3dwj
18599072 Q.Xu, A.A.Canutescu, G.Wang, M.Shapovalov, Z.Obradovic, and R.L.Dunbrack (2008).
Statistical analysis of interface similarity in crystals of homologous proteins.
  J Mol Biol, 381, 487-507.  
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
16921433 I.Morao, G.Periyasamy, I.H.Hillier, and J.A.Joule (2006).
The role of tetrahydrobiopterin in catalysis by nitric oxide synthase.
  Chem Commun (Camb), (), 3525-3527.  
16407211 J.Sudhamsu, and B.R.Crane (2006).
Structure and reactivity of a thermostable prokaryotic nitric-oxide synthase that forms a long-lived oxy-heme complex.
  J Biol Chem, 281, 9623-9632.
PDB code: 2flq
15942729 A.Karlsson, J.V.Parales, R.E.Parales, D.T.Gibson, H.Eklund, and S.Ramaswamy (2005).
NO binding to naphthalene dioxygenase.
  J Biol Inorg Chem, 10, 483-489.
PDB codes: 1uuv 1uuw
15651036 S.B.Kirton, C.W.Murray, M.L.Verdonk, and R.D.Taylor (2005).
Prediction of binding modes for ligands in the cytochromes P450 and other heme-containing proteins.
  Proteins, 58, 836-844.  
15507439 T.W.Ost, and S.Daff (2005).
Thermodynamic and kinetic analysis of the nitrosyl, carbonyl, and dioxy heme complexes of neuronal nitric-oxide synthase. The roles of substrate and tetrahydrobiopterin in oxygen activation.
  J Biol Chem, 280, 965-973.  
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.  
14718923 M.L.Flinspach, H.Li, J.Jamal, W.Yang, H.Huang, J.M.Hah, J.A.Gómez-Vidal, E.A.Litzinger, R.B.Silverman, and T.L.Poulos (2004).
Structural basis for dipeptide amide isoform-selective inhibition of neuronal nitric oxide synthase.
  Nat Struct Mol Biol, 11, 54-59.
PDB codes: 1p6h 1p6i 1p6j 1p6k 1p6l 1p6m 1p6n 1q2o
15166218 V.Berka, G.Wu, H.C.Yeh, G.Palmer, and A.L.Tsai (2004).
Three different oxygen-induced radical species in endothelial nitric-oxide synthase oxygenase domain under regulation by L-arginine and tetrahydrobiopterin.
  J Biol Chem, 279, 32243-32251.  
14681230 Y.Sato, I.Sagami, and T.Shimizu (2004).
Identification of caveolin-1-interacting sites in neuronal nitric-oxide synthase. Molecular mechanism for inhibition of NO formation.
  J Biol Chem, 279, 8827-8836.  
14517970 D.M.Copeland, A.H.West, and G.B.Richter-Addo (2003).
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane.
  Proteins, 53, 182-192.
PDB codes: 1npf 1npg
12655056 J.T.Groves (2003).
The bioinorganic chemistry of iron in oxygenases and supramolecular assemblies.
  Proc Natl Acad Sci U S A, 100, 3569-3574.  
12960153 L.E.Bretscher, H.Li, T.L.Poulos, and O.W.Griffith (2003).
Structural characterization and kinetics of nitric-oxide synthase inhibition by novel N5-(iminoalkyl)- and N5-(iminoalkenyl)-ornithines.
  J Biol Chem, 278, 46789-46797.
PDB codes: 1mmv 1mmw
14514694 M.Sorlie, A.C.Gorren, S.Marchal, T.Shimizu, R.Lange, K.K.Andersson, and B.Mayer (2003).
Single-turnover of nitric-oxide synthase in the presence of 4-amino-tetrahydrobiopterin: proposed role for tetrahydrobiopterin as a proton donor.
  J Biol Chem, 278, 48602-48610.  
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
11719512 A.Slama-Schwok, M.Négrerie, V.Berka, J.C.Lambry, A.L.Tsai, M.H.Vos, and J.L.Martin (2002).
Nitric oxide (NO) traffic in endothelial NO synthase. Evidence for a new NO binding site dependent on tetrahydrobiopterin?
  J Biol Chem, 277, 7581-7586.  
12039005 C.M.Wilmot, and A.R.Pearson (2002).
Cryocrystallography of metalloprotein reaction intermediates.
  Curr Opin Chem Biol, 6, 202-207.  
11823464 Z.Q.Wang, C.C.Wei, and D.J.Stuehr (2002).
A conserved tryptophan 457 modulates the kinetics and extent of N-hydroxy-L-arginine oxidation by inducible nitric-oxide synthase.
  J Biol Chem, 277, 12830-12837.  
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.

 

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