4c12

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X-ray Crystal Structure of Staphylococcus aureus MurE with UDP-MurNAc- Ala-Glu-Lys and ADPX-ray Crystal Structure of Staphylococcus aureus MurE with UDP-MurNAc- Ala-Glu-Lys and ADP

Structural highlights

4c12 is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MURE_STAA8] Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Can not use diaminopimelate as substrate. Seems to have a role in beta-lactam antibiotic resistance.[1] [2] [3]

See Also

References

  1. ITO E, STROMINGER JL. ENZYMATIC SYNTHESIS OF THE PEPTIDE IN BACTERIAL URIDINE NUCLEOTIDES. III. PURIFICATION AND PROPERTIES OF L-LYSIN-ADDING ENZYME. J Biol Chem. 1964 Jan;239:210-4. PMID:14114846
  2. Mengin-Lecreulx D, Falla T, Blanot D, van Heijenoort J, Adams DJ, Chopra I. Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl- L-alanyl-D-glutamate:L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth. J Bacteriol. 1999 Oct;181(19):5909-14. PMID:10498701
  3. Gardete S, Ludovice AM, Sobral RG, Filipe SR, de Lencastre H, Tomasz A. Role of murE in the Expression of beta-lactam antibiotic resistance in Staphylococcus aureus. J Bacteriol. 2004 Mar;186(6):1705-13. PMID:14996801

4c12, resolution 1.80Å

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