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[[ | ==X-ray structure of NikA in complex with Ni-(L-His)2== | ||
<StructureSection load='4i8c' size='340' side='right' caption='[[4i8c]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4i8c]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I8C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I8C FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nikA, b3476, JW3441 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=4i8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i8c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i8c RCSB], [http://www.ebi.ac.uk/pdbsum/4i8c PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/NIKA_ECOLI NIKA_ECOLI]] Involved in a nickel transport system, probably represents the nickel binder. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ABC-type importer NikABCDE mediates nickel acquisition in Escherichia coli. The periplasmic nickel-binding component NikA has a folding similar to that of the peptide transporter OppA and does not bind free nickel. Instead, we showed that the metal is tetra-coordinated by an organic tri-dentate molecule and His416. Conversely, it has been recently reported that NikA binds Ni-((L)-His)(2) and that addition of histidine increases the rate of nickel uptake in vivo. Here, we report the structure of NikA/Ni-((L)-His)(2) and show that histidine binding differs from peptide binding in OppA. The structure also confirms the central role of His416 in nickel binding. | |||
The binding mode of Ni-((L)-His)(2) in NikA revealed by X-ray crystallography.,Lebrette H, Iannello M, Fontecilla-Camps JC, Cavazza C J Inorg Biochem. 2012 Dec 23;121C:16-18. doi: 10.1016/j.jinorgbio.2012.12.010. PMID:23314594<ref>PMID:23314594</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Cavazza, C | [[Category: Cavazza, C]] | ||
[[Category: Fontecilla-Camps, J C | [[Category: Fontecilla-Camps, J C]] | ||
[[Category: Iannello, M | [[Category: Iannello, M]] | ||
[[Category: Lebrette, H | [[Category: Lebrette, H]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 21:43, 25 December 2014
X-ray structure of NikA in complex with Ni-(L-His)2X-ray structure of NikA in complex with Ni-(L-His)2
Structural highlights
Function[NIKA_ECOLI] Involved in a nickel transport system, probably represents the nickel binder. Publication Abstract from PubMedThe ABC-type importer NikABCDE mediates nickel acquisition in Escherichia coli. The periplasmic nickel-binding component NikA has a folding similar to that of the peptide transporter OppA and does not bind free nickel. Instead, we showed that the metal is tetra-coordinated by an organic tri-dentate molecule and His416. Conversely, it has been recently reported that NikA binds Ni-((L)-His)(2) and that addition of histidine increases the rate of nickel uptake in vivo. Here, we report the structure of NikA/Ni-((L)-His)(2) and show that histidine binding differs from peptide binding in OppA. The structure also confirms the central role of His416 in nickel binding. The binding mode of Ni-((L)-His)(2) in NikA revealed by X-ray crystallography.,Lebrette H, Iannello M, Fontecilla-Camps JC, Cavazza C J Inorg Biochem. 2012 Dec 23;121C:16-18. doi: 10.1016/j.jinorgbio.2012.12.010. PMID:23314594[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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