PDBsum entry 1g11

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protein links
Oxidoreductase PDB id
Protein chain
102 a.a. *
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Toluene-4-monooxygenase catalytic effector protein nmr structure
Structure: Toluene-4-monooxygenase catalytic effector. Chain: a. Synonym: toluene-4-monooxygenase system protein d, t4mod. Engineered: yes
Source: Pseudomonas mendocina. Organism_taxid: 300. Strain: kr1. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: H.Hemmi,J.M.Studts,Y.K.Chae,J.Song,J.L.Markley,B.G.Fox
Key ref:
H.Hemmi et al. (2001). Solution structure of the toluene 4-monooxygenase effector protein (T4moD). Biochemistry, 40, 3512-3524. PubMed id: 11297417 DOI: 10.1021/bi0013703
10-Oct-00     Release date:   09-May-01    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q00459  (TMOD_PSEME) -  Toluene-4-monooxygenase system protein D
103 a.a.
102 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   4 terms 
  Biochemical function     oxidoreductase activity     2 terms  


DOI no: 10.1021/bi0013703 Biochemistry 40:3512-3524 (2001)
PubMed id: 11297417  
Solution structure of the toluene 4-monooxygenase effector protein (T4moD).
H.Hemmi, J.M.Studts, Y.K.Chae, J.Song, J.L.Markley, B.G.Fox.
Toluene 4-monooxygenase (T4MO) from Pseudomonas mendocina catalyzes the NADH- and O(2)-dependent hydroxylation of toluene to form p-cresol. The complex consists of an NADH oxidoreductase (T4moF), a Rieske ferredoxin (T4moC), a diiron hydroxylase [T4moH, with (alphabetagamma)(2) quaternary structure], and a catalytic effector protein (T4moD). The solution structure of the 102-amino acid T4moD effector protein has been determined from 2D and 3D (1)H, (13)C, and (15)N NMR spectroscopic data. The structural model was refined through simulated annealing by molecular dynamics in torsion angle space (DYANA software) with input from 1467 experimental constraints, comprising 1259 distance constraints obtained from NOEs, 128 dihedral angle constraints from J-couplings, and 80 hydrogen bond constraints. Of 60 conformers that met the acceptance criteria, the 20 that best satisfied the input constraints were selected to represent the solution structure. With exclusion of the ill-defined N- and C-terminal segments (Ser1-Asn11 and Asp99-Met102), the atomic root-mean-square deviation for the 20 conformers with respect to the mean coordinates was 0.71 A for the backbone and 1.24 A for all non-hydrogen atoms. The secondary structure of T4moD consists of three alpha-helices and seven beta-strands arranged in an N-terminal betaalphabetabeta and a C-terminal betaalphaalphabetabetabeta domain topology. Although the published NMR structures of the methane monooxygenase effector proteins from Methylosinus trichosporium OB3b and Methylococcus capsulatus (Bath) have a similar secondary structure topology, their three-dimensional structures differ from that of T4moD. The major differences in the structures of the three effector proteins are in the relative orientations of the two beta-sheets and the interactions between the alpha-helices in the two domains. The structure of T4moD is closer to that of the methane monooxygenase effector protein from M. capsulatus (Bath) than that from M. trichosporium OB3b. The specificity of T4moD as an effector protein was investigated by replacing it in reconstituted T4MO complexes with effector proteins from monooxygenases from other bacterial species: Pseudomonas pickettii PKO1 (TbuV, toluene 3-monooxygenase); Pseudomonas species JS150 (TbmC, toluene 2-monooxygenase); and Burkeholderia cepacia G4 (S1, toluene 2-monooxygenase). The results showed that the closely related TbuV effector protein (55% sequence identity) provided partial activation of the complex, whereas the more distantly related TbmC (34% sequence identity) and S1 (29% sequence identity) did not. The (1)H NMR chemical shifts of the side-chain amide protons of Asn34, a conserved, structurally relevant amino acid, were found to be similar in spectra of effector proteins T4moD and TbuV but not in the spectrum of TbmC. This suggests that the region around Asn34 may be involved in structural aspects contributing to functional specificity.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19074607 E.Notomista, V.Cafaro, G.Bozza, and A.Di Donato (2009).
Molecular determinants of the regioselectivity of toluene/o-xylene monooxygenase from Pseudomonas sp. strain OX1.
  Appl Environ Microbiol, 75, 823-836.  
19033467 L.J.Bailey, J.G.McCoy, G.N.Phillips, and B.G.Fox (2008).
Structural consequences of effector protein complex formation in a diiron hydroxylase.
  Proc Natl Acad Sci U S A, 105, 19194-19198.
PDB codes: 3dhg 3dhh 3dhi
16627939 L.A.Moe, C.A.Bingman, G.E.Wesenberg, G.N.Phillips, and B.G.Fox (2006).
Structure of T4moC, the Rieske-type ferredoxin component of toluene 4-monooxygenase.
  Acta Crystallogr D Biol Crystallogr, 62, 476-482.
PDB code: 1vm9
17176061 M.H.Sazinsky, P.W.Dunten, M.S.McCormick, A.DiDonato, and S.J.Lippard (2006).
X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, Pseudomonas sp. OX1 phenol hydroxylase.
  Biochemistry, 45, 15392-15404.
PDB codes: 2inn 2inp
16402171 V.Champreda, Y.J.Choi, N.Y.Zhou, and D.J.Leak (2006).
Alteration of the stereo- and regioselectivity of alkene monooxygenase based on coupling protein interactions.
  Appl Microbiol Biotechnol, 71, 840-847.  
15126473 A.Fishman, Y.Tao, and T.K.Wood (2004).
Toluene 3-monooxygenase of Ralstonia pickettii PKO1 is a para-hydroxylating enzyme.
  J Bacteriol, 186, 3117-3123.  
15452777 L.Skjeldal, F.C.Peterson, J.F.Doreleijers, L.A.Moe, J.D.Pikus, W.M.Westler, J.L.Markley, B.F.Volkman, and B.G.Fox (2004).
Solution structure of T4moC, the Rieske ferredoxin component of the toluene 4-monooxygenase complex.
  J Biol Inorg Chem, 9, 945-953.
PDB code: 1sjg
15066815 V.Cafaro, V.Izzo, R.Scognamiglio, E.Notomista, P.Capasso, A.Casbarra, P.Pucci, and A.Di Donato (2004).
Phenol hydroxylase and toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1: interplay between two enzymes.
  Appl Environ Microbiol, 70, 2211-2219.  
12595730 A.M.Orville, J.M.Studts, G.T.Lountos, K.H.Mitchell, and B.G.Fox (2003).
Crystallization and preliminary analysis of native and N-terminal truncated isoforms of toluene-4-monooxygenase catalytic effector protein.
  Acta Crystallogr D Biol Crystallogr, 59, 572-575.  
14550940 J.G.Leahy, P.J.Batchelor, and S.M.Morcomb (2003).
Evolution of the soluble diiron monooxygenases.
  FEMS Microbiol Rev, 27, 449-479.  
11863457 K.H.Mitchell, J.M.Studts, and B.G.Fox (2002).
Combined participation of hydroxylase active site residues and effector protein binding in a para to ortho modulation of toluene 4-monooxygenase regiospecificity.
  Biochemistry, 41, 3176-3188.  
11500872 M.Merkx, D.A.Kopp, M.H.Sazinsky, J.L.Blazyk, J.Müller, and S.J.Lippard (2001).
Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.
  Angew Chem Int Ed Engl, 40, 2782-2807.  
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.