Difference between revisions of "Part:BBa K2194001"

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===Biology===
 
===Biology===
 
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Sulfate-binding protein (SBP) is a periplasmic protein involved in the transmembrane transport of sulfate and thiosulfate. It is a part of the CysUWASbp transport system. True to its name, SBP has a high binding affinity for the sulfate anion, with an equilibrium dissociation constant of K<sub>D</sub> = 0.16 µM [2].  
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Sulfate-binding protein (sbp) is a periplasmic protein involved in the transmembrane transport of sulfate and thiosulfate. It is a part of the cysPUWAsbp transport system. True to its name, sbp has a high binding affinity for the sulfate anion, with an equilibrium dissociation constant of K<sub>D</sub> = 0.16 µM [2].  
 
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SBP also mediates the transport of chromate (CrO<sub>4</sub><sup>2-</sup> [3]. Sulfate transport systems have been shown to be significant in chromium transport and resistance efflux mechanisms [4].
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The sbp protein also mediates the transport of chromate (CrO<sub>4</sub><sup>2-</sup> [3]. Sulfate transport systems have been shown to be significant in chromium transport and resistance efflux mechanisms [4].
 
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Revision as of 00:12, 2 November 2017


Sulfate Binding Protein (sbp) cds

The sbp protein is found in Escherichia coli and specifically binds sulfate and related species (like chromate and selenate) for their transmembrane transport via the ABC transporter system encoded by the cysPUWA genes. BioBrick BBa_K2194001 contains only the cds for this protein.

Biology

Sulfate-binding protein (sbp) is a periplasmic protein involved in the transmembrane transport of sulfate and thiosulfate. It is a part of the cysPUWAsbp transport system. True to its name, sbp has a high binding affinity for the sulfate anion, with an equilibrium dissociation constant of KD = 0.16 µM [2].

The sbp protein also mediates the transport of chromate (CrO42- [3]. Sulfate transport systems have been shown to be significant in chromium transport and resistance efflux mechanisms [4].

  • [1] Ravikumar, I., and Pradyut Ghosh. “Recognition and Separation of Sulfate Anions.” Chemical Society Reviews 41 (2012): 3077–3098. Web. 28 July 2017.
  • [2] Jacobson BL, He JJ, Vermersch PS, Lemon DD, Quiocho FA. “Engineered interdomain disulfide in the periplasmic receptor for sulfate transport reduces flexibility. Site-directed mutagenesis and ligand-binding studies.” J Biol Chem. (1991) Mar 15; 266(8): 5220-5.
  • [3] Karbonowska H, Wiater A, Hulanicka D. “Sulphate permease of Escherichia coli K12.” Acta Biochim Pol. (1977) 24(4): 329-34.
  • [4] Cervantes C, Garcı́a JC, Devars S, Gutiérrez-Corona F, Loza-Tavera Herminia, Torres-Guzmán JC, Moreno-Sánchez R. “Interactions of chromium with microorganisms and plants.” FEMS Microbiology Reviews (2001) 25(3): 335-347

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 3
    Illegal BsaI.rc site found at 1006