The structure of YqeH: An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition

Sudhamsu, J; Lee, G I; Klessig, D F; Crane, B R

doi:10.1074/jbc.M804837200

Title: The structure of YqeH: An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition

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Abstract

AtNOS1/AtNOA1 was identified as a nitric oxide-generating enzyme in plants, but that function has recently been questioned. To resolve issues surrounding AtNOA1 activity, we report the biochemical properties and a 2.36 {angstrom} resolution crystal structure of a bacterial AtNOA1 ortholog (YqeH). Geobacillus YqeH fused to a putative AtNOA1 leader peptide complements growth and morphological defects of Atnoa1 mutant plants. YqeH does not synthesize nitric oxide from L-arginine but rather hydrolyzes GTP. The YqeH structure reveals a circularly permuted GTPase domain and an unusual C-terminal {beta}-domain. A small N-terminal domain, disordered in the structure, binds zinc. Structural homology among the C-terminal domain, the RNA-binding regulator TRAP, and the hypoxia factor pVHL define a recognition module for peptides and nucleic acids. TRAP residues important for RNA binding are conserved by the YqeH C-terminal domain, whose positioning is coupled to GTP hydrolysis. YqeH and AtNOA1 probably act as G-proteins that regulate nucleic acid recognition and not as nitric-oxide synthases.

Authors:

Sudhamsu, J; Lee, G I; Klessig, D F; Crane, B R ^[1]

Cornell

Publication Date:: Fri Mar 27 00:00:00 EDT 2009

Research Org.:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Org.:: USDOE

OSTI Identifier:: 1007070

Resource Type:: Journal Article

Journal Name:: J. Biol. Chem.

Additional Journal Information:: Journal Volume: 283; Journal Issue: (47) ; 11, 2008; Journal ID: ISSN 0021-9258

Country of Publication:: United States

Language:: ENGLISH

Subject:: 36 MATERIALS SCIENCE; ANOXIA; CRYSTAL STRUCTURE; DEFECTS; ENZYMES; GTP-ASES; HYDROLYSIS; MUTANTS; NITRIC OXIDE; NUCLEIC ACIDS; PEPTIDES; POSITIONING; RESIDUES; RESOLUTION; RNA; ZINC

Citation Formats


                    Sudhamsu, J, Lee, G I, Klessig, D F, Crane, B R, and Boyce). The structure of YqeH: An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition.  United States: N. p., 2009. 
        Web.  doi:10.1074/jbc.M804837200.

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                    Sudhamsu, J, Lee, G I, Klessig, D F, Crane, B R, & Boyce). The structure of YqeH: An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition.  United States.  https://doi.org/10.1074/jbc.M804837200

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                    Sudhamsu, J, Lee, G I, Klessig, D F, Crane, B R, and Boyce). 2009.  
        "The structure of YqeH: An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition".  United States.  https://doi.org/10.1074/jbc.M804837200.

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@article{osti_1007070,

  title        = {The structure of YqeH: An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition},

  author       = {Sudhamsu, J and Lee, G I and Klessig, D F and Crane, B R and Boyce)},

  abstractNote = {AtNOS1/AtNOA1 was identified as a nitric oxide-generating enzyme in plants, but that function has recently been questioned. To resolve issues surrounding AtNOA1 activity, we report the biochemical properties and a 2.36 {angstrom} resolution crystal structure of a bacterial AtNOA1 ortholog (YqeH). Geobacillus YqeH fused to a putative AtNOA1 leader peptide complements growth and morphological defects of Atnoa1 mutant plants. YqeH does not synthesize nitric oxide from L-arginine but rather hydrolyzes GTP. The YqeH structure reveals a circularly permuted GTPase domain and an unusual C-terminal {beta}-domain. A small N-terminal domain, disordered in the structure, binds zinc. Structural homology among the C-terminal domain, the RNA-binding regulator TRAP, and the hypoxia factor pVHL define a recognition module for peptides and nucleic acids. TRAP residues important for RNA binding are conserved by the YqeH C-terminal domain, whose positioning is coupled to GTP hydrolysis. YqeH and AtNOA1 probably act as G-proteins that regulate nucleic acid recognition and not as nitric-oxide synthases.},

  doi          = {10.1074/jbc.M804837200},

  url          = {https://www.osti.gov/biblio/1007070},
  journal      = {J. Biol. Chem.},

  issn         = {0021-9258},

  number       = (47) ; 11, 2008,

  volume       = 283,

  place        = {United States},

  year         = {Fri Mar 27 00:00:00 EDT 2009},

  month        = {Fri Mar 27 00:00:00 EDT 2009}

}

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