2uvk

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Structure of YjhT

Structural highlights

2uvk is a 2 chain structure with sequence from Escherichia coli BL21. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:MSE
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NANM_ECOLI Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses.[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

The acquisition of host-derived sialic acid is an important virulence factor for some bacterial pathogens, but in vivo this sugar acid is sequestered in sialoconjugates as the alpha-anomer. In solution, however, sialic acid is present mainly as the beta-anomer, formed by a slow spontaneous mutarotation. We studied the Escherichia coli protein YjhT as a member of a family of uncharacterized proteins present in many sialic acid-utilizing pathogens. This protein is able to accelerate the equilibration of the alpha- and beta-anomers of the sialic acid N-acetylneuraminic acid, thus describing a novel sialic acid mutarotase activity. The structure of this periplasmic protein, solved to 1.5A resolution, reveals a dimeric 6-bladed unclosed beta-propeller, the first of a bacterial Kelch domain protein. Mutagenesis of conserved residues in YjhT demonstrated an important role for Glu-209 and Arg-215 in mutarotase activity. We also present data suggesting that the ability to utilize alpha-N-acetylneuraminic acid released from complex sialoconjugates in vivo provides a physiological advantage to bacteria containing YjhT.

Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT.,Severi E, Muller A, Potts JR, Leech A, Williamson D, Wilson KS, Thomas GH J Biol Chem. 2008 Feb 22;283(8):4841-9. Epub 2007 Dec 5. PMID:18063573[2]

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

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Citations
4 reviews cite this structure
Nontypeable Haemophilus influenzae: the role of N-acetyl-5-neuraminic acid in biology.
Apicella et al. (2012)
3 more
37 other articles
No citations found

References

  1. ↑ Severi E, Muller A, Potts JR, Leech A, Williamson D, Wilson KS, Thomas GH. Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT. J Biol Chem. 2008 Feb 22;283(8):4841-9. Epub 2007 Dec 5. PMID:18063573 doi:10.1074/jbc.M707822200
  2. ↑ Severi E, Muller A, Potts JR, Leech A, Williamson D, Wilson KS, Thomas GH. Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT. J Biol Chem. 2008 Feb 22;283(8):4841-9. Epub 2007 Dec 5. PMID:18063573 doi:10.1074/jbc.M707822200

Contents


PDB ID 2uvk

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