1zlq
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1zlq |SIZE=350|CAPTION= <scene name='initialview01'>1zlq</scene>, resolution 1.8Å | |PDB= 1zlq |SIZE=350|CAPTION= <scene name='initialview01'>1zlq</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |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> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= nikA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= nikA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Lemaire, D.]] | [[Category: Lemaire, D.]] | ||
[[Category: Martin, L.]] | [[Category: Martin, L.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: DTT]] | ||
| - | [[Category: EDT]] | ||
| - | [[Category: FE]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO4]] | ||
[[Category: bacteria]] | [[Category: bacteria]] | ||
[[Category: edta]] | [[Category: edta]] | ||
| Line 43: | Line 39: | ||
[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:38:27 2008'' |
Revision as of 22:38, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Gene: | nikA (Escherichia coli) | ||||||
| Activity: | Nickel-transporting ATPase, with EC number 3.6.3.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 01:38:27 2008
