3EC1

Structure of YqeH GTPase from Geobacillus stearothermophilus (an AtNOS1 / AtNOA1 ortholog)

Summary for 3EC1

• Entry DOI: 10.2210/pdb3ec1/pdb
• Descriptor: GTP-binding protein YqeH required for biosis of 30S ribosome subunit, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: yqeh, atnos1, atnoa1, gtpase, trap, pvhl, hydrolase, signaling protein
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 2
• Total formula weight: 83131.39

Authors

Sudhamsu, J.,Crane, B.R. (deposition date: 2008-08-28, release date: 2008-10-21, Last modification date: 2024-02-21)

Primary citation

Sudhamsu, J.,Lee, G.I.,Klessig, D.F.,Crane, B.R.
The structure of YqeH. An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition.
J.Biol.Chem., 283:32968-32976, 2008

PubMed 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 A 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.

PubMed: 18801747
DOI: 10.1074/jbc.M804837200

Experimental method

X-RAY DIFFRACTION (2.36 Å)