1zlq

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[[Image:1zlq.gif|left|200px]]
[[Image:1zlq.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1zlq |SIZE=350|CAPTION= <scene name='initialview01'>1zlq</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1zlq", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=EDT:{[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC+ACID'>EDT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nickel-transporting_ATPase Nickel-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.24 3.6.3.24] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= nikA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1zlq| PDB=1zlq | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zlq OCA], [http://www.ebi.ac.uk/pdbsum/1zlq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zlq RCSB]</span>
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}}
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'''Crystallographic and spectroscopic evidence for high affinity binding of Fe EDTA (H2O)- to the periplasmic nickel transporter NikA'''
'''Crystallographic and spectroscopic evidence for high affinity binding of Fe EDTA (H2O)- to the periplasmic nickel transporter NikA'''
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[[Category: Lemaire, D.]]
[[Category: Lemaire, D.]]
[[Category: Martin, L.]]
[[Category: Martin, L.]]
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[[Category: bacteria]]
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[[Category: Bacteria]]
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[[Category: edta]]
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[[Category: Edta]]
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[[Category: nickel]]
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[[Category: Nickel]]
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[[Category: periplasm]]
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[[Category: Periplasm]]
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[[Category: transport]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:46:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:38:27 2008''
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Revision as of 14:46, 3 May 2008

Image:1zlq.gif

Template:STRUCTURE 1zlq

Crystallographic and spectroscopic evidence for high affinity binding of Fe EDTA (H2O)- to the periplasmic nickel transporter NikA


Overview

Because nickel is both essential and toxic to a great variety of organisms, its detection and transport is highly regulated. In Escherichia coli and other related Gram-negative bacteria, high affinity nickel transport depends on proteins expressed by the nik operon. A central actor of this process is the periplasmic NikA transport protein. A previous structural report has proposed that nickel binds to NikA as a pentahydrate species. However, both stereochemical considerations and X-ray absorption spectroscopic results are incompatible with that interpretation. Here, we report the 1.8 A resolution structure of NikA and show that it binds FeEDTA(H2O)- with very high affinity. In addition, we provide crystallographic evidence that a metal-EDTA complex was also bound to the previously reported NikA structure. Our observations strongly suggest that nickel transport in E. coli requires the binding of this metal ion to a metallophore that bears significant resemblance to EDTA. They also provide a basis for the potential use of NikA in the bioremediation of toxic transition metals and the design of artificial metalloenzymes.

About this Structure

1ZLQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystallographic and spectroscopic evidence for high affinity binding of FeEDTA(H2O)- to the periplasmic nickel transporter NikA., Cherrier MV, Martin L, Cavazza C, Jacquamet L, Lemaire D, Gaillard J, Fontecilla-Camps JC, J Am Chem Soc. 2005 Jul 20;127(28):10075-82. PMID:16011372 Page seeded by OCA on Sat May 3 17:46:42 2008

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