3fxb

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Crystal structure of the ectoine-binding protein UehACrystal structure of the ectoine-binding protein UehA

Structural highlights

3fxb is a 2 chain structure with sequence from Ruegeria pomeroyi DSS-3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UEHA_RUEPO Part of the tripartite ATP-independent periplasmic (TRAP) transport system UehABC, which imports both ectoine and 5-hydroxyectoine as nutrients, and not as osmoprotectants. UehA binds both ectoine and 5-hydroxyectoine with high specificity and affinity.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Substrate-binding proteins or extracellular solute receptors (ESRs) are components of both ABC (ATP binding cassette) and TRAP-T (tripartite ATP-independent periplasmic transporter). The TRAP-T system UehABC from Silicibacter pomeroyi DSS-3 imports the compatible solutes ectoine and 5-hydroxyectoine as nutrients. UehA, the ESR of the UehABC operon, binds both ectoine and 5-hydroxyectoine with high affinity (K(d) values of 1.4+/-0.1 and 1.1+/-0.1 microM, respectively) and delivers them to the TRAP-T complex. The crystal structure of UehA in complex with ectoine was determined at 2.9-A resolution and revealed an overall fold common for all ESR proteins from TRAP systems determined so far. A comparison of the recently described structure of TeaA from Halomonas elongata and an ectoine-binding protein (EhuB) from an ABC transporter revealed a conserved ligand binding mode that involves both directed and cation-pi interactions. Furthermore, a comparison with other known TRAP-T ESRs revealed a helix that might act as a selectivity filter imposing restraints on the ESRs that fine-tune ligand recognition and binding and finally might determine the selection of the cognate substrate.

The crystal structure of UehA in complex with ectoine-A comparison with other TRAP-T binding proteins.,Lecher J, Pittelkow M, Zobel S, Bursy J, Bonig T, Smits SH, Schmitt L, Bremer E J Mol Biol. 2009 May 29;389(1):58-73. Epub 2009 Apr 10. PMID:19362561[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Lecher J, Pittelkow M, Zobel S, Bursy J, Bonig T, Smits SH, Schmitt L, Bremer E. The crystal structure of UehA in complex with ectoine-A comparison with other TRAP-T binding proteins. J Mol Biol. 2009 May 29;389(1):58-73. Epub 2009 Apr 10. PMID:19362561 doi:10.1016/j.jmb.2009.03.077
  2. Lecher J, Pittelkow M, Zobel S, Bursy J, Bonig T, Smits SH, Schmitt L, Bremer E. The crystal structure of UehA in complex with ectoine-A comparison with other TRAP-T binding proteins. J Mol Biol. 2009 May 29;389(1):58-73. Epub 2009 Apr 10. PMID:19362561 doi:10.1016/j.jmb.2009.03.077

3fxb, resolution 2.90Å

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