3na7

<StructureSection load='3na7' size='340' side='right' caption='[[3na7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[3na7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori_(strain_nctc11638) Helicobacter pylori (strain nctc11638)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NA7 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP0958 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=102619 Helicobacter pylori (strain NCTC11638)])</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=3na7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3na7 OCA], [http://pdbe.org/3na7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3na7 RCSB], [http://www.ebi.ac.uk/pdbsum/3na7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3na7 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

We have determined the 2.2-A structure of the HP0958 protein from the human gastric pathogen Helicobacter pylori. HP0958 is essential for flagellum formation and motility. It functions as a chaperone for RpoN (sigma(54)) and also controls the stability and translation of mRNA for the major flagellin subunit FlaA. The protein is composed of a highly elongated and kinked coiled-coil hairpin domain (residues 1-170), followed by a C(4) Zn-ribbon domain (residues 174-238). The Zn-ribbon domain is rich in aromatic and positively charged amino acid residues. Electrophoretic mobility shift assays identified residues in a positively charged region of the Zn-ribbon domain of HP0958 whose mutation alters the mobility of an HP0958-flaA mRNA complex. Mutation of surface residues in the coiled-coil domain did not result in an observable change in the mobility of the HP0958-flaA transcript complex. The data thus suggest the arrangement of HP0958 into distinct structural and functional domains.

The 2.2-A structure of the HP0958 protein from Helicobacter pylori reveals a kinked anti-parallel coiled-coil hairpin domain and a highly conserved ZN-ribbon domain.,Caly DL, O'Toole PW, Moore SA J Mol Biol. 2010 Oct 29;403(3):405-19. Epub 2010 Sep 6. PMID:20826163<ref>PMID:20826163</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 3na7" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Caly, D L]]

[[Category: Moore, S A]]

[[Category: Toole, P W.O]]

[[Category: C4 zn-ribbon]]

[[Category: Chaperone]]

[[Category: Post-transcriptional]]