NiCoT family: Difference between revisions
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Proteins currently known to belong to the '''Ni<sup>2+</sup>-Co<sup>2+</sup> Transporter (NiCoT) |
Proteins currently known to belong to the '''Ni<sup>2+</sup>-Co<sup>2+</sup> Transporter (NiCoT) family''' ([http://www.tcdb.org/search/result.php?tc=2.A.52 TC# 2.A.52]) can be found in organisms ranging from [[Gram-negative bacteria|Gram-negative]] and [[Gram-positive bacteria]] to [[archaea]] and some [[eukaryotes]]. Members of this family catalyze uptake of [[nickel|Ni<sup>2+</sup>]] and/or [[Cobalt|Co<sup>2+</sup>]] in a [[proton motive force]]-dependent process.<ref name="TCDB">{{cite web|last1=Saier|first1=Milton|title=Transporter Classification Database: 2.A.52 The Ni2+-Co2+ Transporter (NiCoT) Family|url=http://www.tcdb.org/search/result.php?tc=2.a.52|website=tcdb.org|accessdate=4 January 2016}}</ref> |
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==Structure== |
==Structure== |
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These proteins range in size from about 300 to 400 amino acyl residues and possess 7 or 8 transmembrane segments (TMSs) thought to result from [[Intragenic region|intragenic]] 4 TMS duplication, followed by a deletion in the case of the 7 TMS variety. Topological analyses with the HoxN Ni<sup>2+</sup> transporter of Ralstonia eutropha (Alcaligenes eutrophus) suggest that it possesses 8 TMSs with its N- and C-termini in the cytoplasm. The Co<sup>2+</sup> (Ni<sup>2+</sup>) transporter of Rhodococcus rhodochrous, NhlF, exhibits eight putative TMSs, and eight apparent TMSs are revealed by a [[hydropathy]] analysis of the [[Multiple sequence alignment|multiple alignment]] of the NiCoT family protein sequences. An HX4DH sequence in helix 2 of the HoxN protein has been implicated in Ni<sup>2+</sup> binding, and both helix 1 and helix 2 which interact spatially, form the selectivity filter.<ref name="Degan Eitinger">{{cite journal|last1=Degen|first1=O|last2=Eitinger|first2=T|title=Substrate specificity of nickel/cobalt permeases: insights from mutants altered in transmembrane domains I and II.|journal=J Bacteriol.|date=July 2002|volume=184|issue=13|pages=3569–77|pmid=12057951}}</ref> In the H. pylori NixA homologue, several conserved motifs have been shown to be important for Ni<sup>2+</sup> binding and transport.<ref name=TCDB/><ref name="W and B">{{cite journal|last1=Wolfram|first1=L|last2=Bauerfeind|first2=P|title=Conserved low-affinity nickel-binding amino acids are essential for the function of the nickel permease NixA of Helicobacter pylori |
These proteins range in size from about 300 to 400 amino acyl residues and possess 7 or 8 transmembrane segments (TMSs) thought to result from [[Intragenic region|intragenic]] 4 TMS duplication, followed by a deletion in the case of the 7 TMS variety. Topological analyses with the HoxN Ni<sup>2+</sup> transporter of ''Ralstonia eutropha'' (''Alcaligenes eutrophus'') suggest that it possesses 8 TMSs with its N- and C-termini in the cytoplasm. The Co<sup>2+</sup> (Ni<sup>2+</sup>) transporter of ''Rhodococcus rhodochrous'', NhlF, exhibits eight putative TMSs, and eight apparent TMSs are revealed by a [[hydropathy]] analysis of the [[Multiple sequence alignment|multiple alignment]] of the NiCoT family protein sequences. An HX4DH sequence in helix 2 of the HoxN protein has been implicated in Ni<sup>2+</sup> binding, and both helix 1 and helix 2 which interact spatially, form the selectivity filter.<ref name="Degan Eitinger">{{cite journal|last1=Degen|first1=O|last2=Eitinger|first2=T|title=Substrate specificity of nickel/cobalt permeases: insights from mutants altered in transmembrane domains I and II.|journal=J Bacteriol.|date=July 2002|volume=184|issue=13|pages=3569–77|pmc=135128|pmid=12057951}}</ref> In the H. pylori NixA homologue, several conserved motifs have been shown to be important for Ni<sup>2+</sup> binding and transport.<ref name="TCDB" /><ref name="W and B">{{cite journal|last1=Wolfram|first1=L|last2=Bauerfeind|first2=P|title=Conserved low-affinity nickel-binding amino acids are essential for the function of the nickel permease NixA of ''Helicobacter pylori'' |journal=J Bacteriol.|date=March 2002|volume=184|issue=5|pages=1438–43|doi=10.1128/JB.184.5.1438-1443.2002 |pmid=11844775}}</ref> |
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At least one crystal structure is known, found by Yu et al.,<ref>{{cite journal|last1=Yu|first1=Y|last2=Zhou|first2=M|last3=Kirsch|first3=F|last4=Xu|first4=C|last5=Zhang|first5=L|last6=Wang|first6=Y|last7=Jiang|first7=Z|last8=Wang|first8=N|last9=Li|first9=J|last10=Eitinger|first10=T|last11=Yang|first11=M|title=Planar substrate-binding site dictates the specificity of ECF-type nickel/cobalt transporters|journal=Cell research|date=December 24, 2013|volume=24|issue=3|pages=267–277|doi=10.1038/cr.2013.172|pmid=24366337}}</ref> available at {{PDB|4M58}}. |
At least one crystal structure is known, found by Yu et al.,<ref>{{cite journal|last1=Yu|first1=Y|last2=Zhou|first2=M|last3=Kirsch|first3=F|last4=Xu|first4=C|last5=Zhang|first5=L|last6=Wang|first6=Y|last7=Jiang|first7=Z|last8=Wang|first8=N|last9=Li|first9=J|last10=Eitinger|first10=T|last11=Yang|first11=M|title=Planar substrate-binding site dictates the specificity of ECF-type nickel/cobalt transporters|journal=Cell research|date=December 24, 2013|volume=24|issue=3|pages=267–277|doi=10.1038/cr.2013.172|pmid=24366337}}</ref> available at {{PDB|4M58}}. |
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==Reaction== |
==Reaction== |
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The overall reaction catalyzed by the proteins of the NiCoT family is:<ref name=TCDB/> |
The overall reaction catalyzed by the proteins of the NiCoT family is:<ref name="TCDB" /> |
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::[Ni<sup>2+</sup> and/or Co<sup>2+</sup>] (out) → [Ni<sup>2+</sup> and/or Co<sup>2+</sup>] (in). |
::[Ni<sup>2+</sup> and/or Co<sup>2+</sup>] (out) → [Ni<sup>2+</sup> and/or Co<sup>2+</sup>] (in). |
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Revision as of 20:15, 5 January 2016
Proteins currently known to belong to the Ni2+-Co2+ Transporter (NiCoT) family (TC# 2.A.52) can be found in organisms ranging from Gram-negative and Gram-positive bacteria to archaea and some eukaryotes. Members of this family catalyze uptake of Ni2+ and/or Co2+ in a proton motive force-dependent process.[1]
Structure
These proteins range in size from about 300 to 400 amino acyl residues and possess 7 or 8 transmembrane segments (TMSs) thought to result from intragenic 4 TMS duplication, followed by a deletion in the case of the 7 TMS variety. Topological analyses with the HoxN Ni2+ transporter of Ralstonia eutropha (Alcaligenes eutrophus) suggest that it possesses 8 TMSs with its N- and C-termini in the cytoplasm. The Co2+ (Ni2+) transporter of Rhodococcus rhodochrous, NhlF, exhibits eight putative TMSs, and eight apparent TMSs are revealed by a hydropathy analysis of the multiple alignment of the NiCoT family protein sequences. An HX4DH sequence in helix 2 of the HoxN protein has been implicated in Ni2+ binding, and both helix 1 and helix 2 which interact spatially, form the selectivity filter.[2] In the H. pylori NixA homologue, several conserved motifs have been shown to be important for Ni2+ binding and transport.[1][3]
At least one crystal structure is known, found by Yu et al.,[4] available at PDB: 4M58.
Reaction
The overall reaction catalyzed by the proteins of the NiCoT family is:[1]
- [Ni2+ and/or Co2+] (out) → [Ni2+ and/or Co2+] (in).
Proteins
Several known proteins belong to the Ni2+-Co2+ Transporter (NiCoT) Family. A complete list of these proteins along with their transporter classification identification number (TCID), domain, kingdom/phylum, and some examples can be found in the Transporter Classification Database.
References
- ^ a b c Saier, Milton. "Transporter Classification Database: 2.A.52 The Ni2+-Co2+ Transporter (NiCoT) Family". tcdb.org. Retrieved 4 January 2016.
- ^ Degen, O; Eitinger, T (July 2002). "Substrate specificity of nickel/cobalt permeases: insights from mutants altered in transmembrane domains I and II". J Bacteriol. 184 (13): 3569–77. PMC 135128. PMID 12057951.
- ^ Wolfram, L; Bauerfeind, P (March 2002). "Conserved low-affinity nickel-binding amino acids are essential for the function of the nickel permease NixA of Helicobacter pylori". J Bacteriol. 184 (5): 1438–43. doi:10.1128/JB.184.5.1438-1443.2002. PMID 11844775.
- ^ Yu, Y; Zhou, M; Kirsch, F; Xu, C; Zhang, L; Wang, Y; Jiang, Z; Wang, N; Li, J; Eitinger, T; Yang, M (December 24, 2013). "Planar substrate-binding site dictates the specificity of ECF-type nickel/cobalt transporters". Cell research. 24 (3): 267–277. doi:10.1038/cr.2013.172. PMID 24366337.
Further reading
- Deng, X; He, J; He, N (February 2013). "Comparative study on Ni(2+)-affinity transport of nickel/cobalt permeases (NiCoTs) and the potential of recombinant Escherichia coli for Ni(2+) bioaccumulation". Bioresour Technol. 130: 69–74. doi:10.1016/j.biortech.2012.11.133. PMID 23306112.
- Rodionov, D; Hebbeln, P; Gelfand, M; Eitinger, T (January 2006). "Comparative and Functional Genomic Analysis of Prokaryotic Nickel and Cobalt Uptake Transporters: Evidence for a Novel Group of ATP-Binding Cassette Transporters". Journal of Bacteriology. 188 (1): 317–327. doi:10.1128/JB.188.1.317-327.2006. PMC 1317602. PMID 16352848.