4oev: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==Crystal structure of NikZ from Campylobacter jejuni in complex with Ni(II) ion== | ||
<StructureSection load='4oev' size='340' side='right' caption='[[4oev]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4oev]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OEV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OEV FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oet|4oet]], [[4oeu|4oeu]]</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=4oev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oev OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oev RCSB], [http://www.ebi.ac.uk/pdbsum/4oev 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]] | |||
[[Category: Extracytoplasmic nickel-binding protein]] | |||
[[Category: Metal transport]] | |||
[[Category: Nickel import]] | |||
[[Category: Transport protein]] | |||
Revision as of 03:17, 2 October 2014
Crystal structure of NikZ from Campylobacter jejuni in complex with Ni(II) ionCrystal structure of NikZ from Campylobacter jejuni in complex with Ni(II) ion
Structural highlights
Publication Abstract from PubMedIn 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||