3tja

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Current revision (13:30, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3tja' size='340' side='right'caption='[[3tja]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3tja' size='340' side='right'caption='[[3tja]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tja]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TJA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tja]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TJA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tj8|3tj8]], [[3tj9|3tj9]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ureE, HP_0070 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tja OCA], [https://pdbe.org/3tja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tja RCSB], [https://www.ebi.ac.uk/pdbsum/3tja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tja ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tja OCA], [https://pdbe.org/3tja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tja RCSB], [https://www.ebi.ac.uk/pdbsum/3tja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tja ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/UREE_HELPY UREE_HELPY]] Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly (By similarity).
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[https://www.uniprot.org/uniprot/UREE_HELPY UREE_HELPY] Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The survival and growth of the pathogen Helicobacter pylori in the gastric acidic environment is ensured by the activity of urease, an enzyme containing two essential Ni2+ ions in the active site. The metallo-chaperone UreE facilitates in vivo Ni2+ insertion into the apo-enzyme. Crystals of apo-HpUreE and its Ni2+ and Zn2+ bound forms were obtained from protein solutions in the absence and presence of the metal ions. The crystal structures of the homodimeric protein, determined at 2.00 A (apo), 1.59 A (Ni) and 2.52 A (Zn) resolution, show the conserved proximal and solvent-exposed His102 residues from two adjacent monomers invariably involved in metal binding. The C-terminal regions of the apo-protein are disordered in the crystal, but acquire significant ordering in the presence of the metal ions due to the binding of His152. The analysis of X-ray absorption spectral data obtained on solutions of Ni2+- and Zn2+-HpUreE provided accurate information of the metal ion environment in the absence of solid-state effects. These results reveal the role of the histidine residues at the protein C-terminus in metal ion binding, and the mutual influence of protein framework and metal ion stereo-electronic properties in establishing coordination number and geometry leading to metal selectivity.
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Crystallographic and X-ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni2+ and Zn2+ reveal a role for the disordered C-terminal arm in metal trafficking.,Banaszak K, Martin-Diaconescu V, Bellucci M, Zambelli B, Rypniewski W, Maroney MJ, Ciurli S Biochem J. 2011 Oct 20. PMID:22010876<ref>PMID:22010876</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3tja" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Urease accessory protein|Urease accessory protein]]
*[[Urease accessory protein|Urease accessory protein]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43504]]
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[[Category: Helicobacter pylori]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Banaszak, K]]
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[[Category: Banaszak K]]
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[[Category: Bellucci, M]]
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[[Category: Bellucci M]]
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[[Category: Ciurli, S]]
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[[Category: Ciurli S]]
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[[Category: Rypniewski, W R]]
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[[Category: Rypniewski WR]]
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[[Category: Zambelli, B]]
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[[Category: Zambelli B]]
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[[Category: Metal binding protein]]
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Current revision

Crystal structure of Helicobacter pylori UreE in the apo form

PDB ID 3tja

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