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