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4ofl
From Proteopedia
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| - | ''' | + | ==Crystal structure of YntA from Yersinia pestis in complex with Ni(L-His)2== |
| + | <StructureSection load='4ofl' size='340' side='right' caption='[[4ofl]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ofl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OFL FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ofo|4ofo]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ofl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ofl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ofl RCSB], [http://www.ebi.ac.uk/pdbsum/4ofl PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In human pathogenic bacteria, nickel is required for the activation of two enzymes, urease and [NiFe]-hydrogenase, necessary for host infection. Acquisition of Ni(II) is mediated by either permeases or ABC-importers, the latter including a subclass that involves an extracytoplasmic nickel-binding protein, Ni-BP. This study reports on the structure of three Ni-BPs from a diversity of human pathogens and on the existence of three new nickel-binding motifs. These are different from that previously described for Escherichia coli Ni-BP NikA, known to bind nickel via a nickelophore, and indicate a variegated ligand selectivity for Ni-BPs. The structures are consistent with ligand affinities measured in solution by calorimetry and challenge the hypothesis of a general requirement of nickelophores for nickel uptake by canonical ABC importers. Phylogenetic analyses showed that Ni-BPs have different evolutionary origins and emerged independently from peptide-binding proteins, possibly explaining the promiscuous behavior of this class of Ni(II) carriers. | ||
| - | + | Promiscuous Nickel Import in Human Pathogens: Structure, Thermodynamics, and Evolution of Extracytoplasmic Nickel-Binding Proteins.,Lebrette H, Brochier-Armanet C, Zambelli B, de Reuse H, Borezee-Durant E, Ciurli S, Cavazza C Structure. 2014 Sep 3. pii: S0969-2126(14)00243-3. doi:, 10.1016/j.str.2014.07.012. PMID:25199691<ref>PMID:25199691</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cavazza, C.]] | ||
| + | [[Category: Lebrette, H.]] | ||
| + | [[Category: Abc-type importer]] | ||
| + | [[Category: Extracytoplasmic nickel-binding protein]] | ||
| + | [[Category: Nickel import]] | ||
| + | [[Category: Periplasmic]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 00:18, 2 October 2014
Crystal structure of YntA from Yersinia pestis in complex with Ni(L-His)2
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