Specific recognition of N-acetylated substrates and domain flexibility in WbgU: a UDP-GalNAc 4-epimeraseSpecific recognition of N-acetylated substrates and domain flexibility in WbgU: a UDP-GalNAc 4-epimerase

Structural highlights

3ruc is a 4 chain structure with sequence from Plesiomonas shigelloides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GNE_PLESH Catalyzes the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP-GalNAc). Has very low epimerase activity with UDP-Glc and UDP-Gal. Plays a role in the biosynthesis of 2-acetamino-2-deoxy-L-altruronic acid, a building block of the O-antigen in bacterial lipopolysaccharide (LPS).[1] [2]

See Also

References

  1. Kowal P, Wang PG. New UDP-GlcNAc C4 epimerase involved in the biosynthesis of 2-acetamino-2-deoxy-L-altruronic acid in the O-antigen repeating units of Plesiomonas shigelloides O17. Biochemistry. 2002 Dec 24;41(51):15410-4. PMID:12484781 doi:10.1021/bi026384i
  2. Bhatt VS, Guan W, Xue M, Yuan H, Wang PG. Insights into role of the hydrogen bond networks in substrate recognition by UDP-GalNAc 4-epimerases. Biochem Biophys Res Commun. 2011 Aug 26;412(2):232-7. PMID:21810411 doi:10.1016/j.bbrc.2011.07.071

3ruc, resolution 2.10Å

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