3ec1

<StructureSection load='3ec1' size='340' side='right' caption='[[3ec1]], [[Resolution|resolution]] 2.36&Aring;' scene=''>

<table><tr><td colspan='2'>[[3ec1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EC1 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ec1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ec1 OCA], [http://pdbe.org/3ec1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ec1 RCSB], [http://www.ebi.ac.uk/pdbsum/3ec1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ec1 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

The structure of YqeH. An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition.,Sudhamsu J, Lee GI, Klessig DF, Crane BR J Biol Chem. 2008 Nov 21;283(47):32968-76. Epub 2008 Sep 18. PMID:18801747<ref>PMID:18801747</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3ec1" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 12980]]

[[Category: Crane, B R]]

[[Category: Sudhamsu, J]]

[[Category: Atnoa1]]

[[Category: Yqeh]]