3o1q

<StructureSection load='3o1q' size='340' side='right' caption='[[3o1q]], [[Resolution|resolution]] 1.85&Aring;' scene=''>

<table><tr><td colspan='2'>[[3o1q]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O1Q FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wgl|2wgl]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ureF, HP_0069 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</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=3o1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1q OCA], [http://pdbe.org/3o1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o1q RCSB], [http://www.ebi.ac.uk/pdbsum/3o1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1q ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/UREF_HELPY UREF_HELPY]] Required for maturation of urease via the functional incorporation of the urease nickel metallocenter (By similarity).[HAMAP-Rule:MF_01385]

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== Publication Abstract from PubMed ==

Colonization of Helicobacter pylori in the acidic environment of the human stomach depends on the neutralizing activity of urease. Activation of apo-urease involves carboxylation of lysine 219 and insertion of two nickel ions. In H. pylori, this maturation process involves four urease accessory proteins as follows: UreE, UreF, UreG, and UreH. It is postulated that the apo-urease interacts with UreF, UreG, and UreH to form a pre-activation complex that undergoes GTP-dependent activation of urease. The crystal structure of the UreF-UreH complex reveals conformational changes in two distinct regions of UreF upon complex formation. First, the flexible C-terminal residues of UreF become ordered, forming an extra helix alpha10 and a loop structure stabilized by hydrogen bonds involving Arg-250. Second, the first turn of helix alpha2 uncoils to expose a conserved residue, Tyr-48. Substitution of R250A or Y48A in UreF abolishes the formation of the heterotrimeric complex of UreG-UreF-UreH and abolishes urease maturation. Our results suggest that the C-terminal residues and helix alpha2 of UreF are essential for the recruitment of UreG for the formation of the pre-activation complex. The molecular mass of the UreF-UreH complex determined by static light scattering was 116 +/- 2.3 kDa, which is consistent with the quaternary structure of a dimer of heterodimers observed in the crystal structure. Taking advantage of the unique 2-fold symmetry observed in both the crystal structures of H. pylori urease and the UreF-UreH complex, we proposed a topology model of the pre-activation complex for urease maturation.

Assembly of Preactivation Complex for Urease Maturation in Helicobacter pylori: CRYSTAL STRUCTURE OF UreF-UreH PROTEIN COMPLEX.,Fong YH, Wong HC, Chuck CP, Chen YW, Sun H, Wong KB J Biol Chem. 2011 Dec 16;286(50):43241-9. Epub 2011 Oct 19. PMID:22013070<ref>PMID:22013070</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 3o1q" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 43504]]

[[Category: Chen, Y W]]

[[Category: Fong, Y H]]

[[Category: Wong, K B]]

[[Category: Metal binding protein]]

[[Category: Urease maturation]]