{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sudhamsu J"],"funding":["NIGMS NIH HHS"],"pagination":["32968-76"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2583316"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["283(47)"],"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 m"],"journal":["The Journal of biological chemistry"],"pubmed_title":["The structure of YqeH. An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition."],"pmcid":["PMC2583316"],"funding_grant_id":["5R01GM067011"],"pubmed_authors":["Crane BR","Klessig DF","Lee GI","Sudhamsu J"],"additional_accession":[]},"is_claimable":false,"name":"The structure of YqeH. An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition.","description":"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 m","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Nov","modification":"2026-04-13T21:11:39.701Z","creation":"2019-03-27T00:19:22Z"},"accession":"S-EPMC2583316","cross_references":{"pubmed":["18801747"],"doi":["10.1074/jbc.m804837200","10.1074/jbc.M804837200"]}}