PDBsum entry 1xe4

Go to PDB code: 
protein metals links
Transferase PDB id
Jmol PyMol
Protein chain
335 a.a. *
Waters ×366
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of weissella viridescens femx (k36m) mutant
Structure: Femx. Chain: a. Engineered: yes. Mutation: yes
Source: Weissella viridescens. Organism_taxid: 1629. Gene: femx. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.95Å     R-factor:   0.196     R-free:   0.233
Authors: S.Biarrotte-Sorin,A.P.Maillard,M.Arthur,C.Mayer
Key ref: A.P.Maillard et al. (2005). Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens. J Bacteriol, 187, 3833-3838. PubMed id: 15901708
09-Sep-04     Release date:   31-May-05    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9EY50  (Q9EY50_LACVI) -  UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase
336 a.a.
335 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-alanyl-tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L- lysyl-D-alanyl-D-alanine = tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L- alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
+ UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L- lysyl-D-alanyl-D-alanine
= tRNA(Ala)
+ UDP-N-acetyl-alpha-D-muramoyl-L- alanyl-D-glutamyl-N(6)-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cell wall organization   4 terms 
  Biochemical function     transferase activity     4 terms  


    Added reference    
J Bacteriol 187:3833-3838 (2005)
PubMed id: 15901708  
Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens.
A.P.Maillard, S.Biarrotte-Sorin, R.Villet, S.Mesnage, A.Bouhss, W.Sougakoff, C.Mayer, M.Arthur.
Weissella viridescens FemX (FemX(Wv)) belongs to the Fem family of nonribosomal peptidyl transferases that use aminoacyl-tRNA as the amino acid donor to synthesize the peptide cross-bridge found in the peptidoglycan of many species of pathogenic gram-positive bacteria. We have recently solved the crystal structure of FemX(Wv) in complex with the peptidoglycan precursor UDP-MurNAc-pentapeptide and report here the site-directed mutagenesis of nine residues located in the binding cavity for this substrate. Two substitutions, Lys36Met and Arg211Met, depressed FemX(Wv) transferase activity below detectable levels without affecting protein folding. Analogues of UDP-MurNAc-pentapeptide lacking the phosphate groups or the C-terminal D-alanyl residues were not substrates of the enzyme. These results indicate that Lys36 and Arg211 participate in a complex hydrogen bond network that connects the C-terminal D-Ala residues to the phosphate groups of UDP-MurNAc-pentapeptide and constrains the substrate in a conformation that is essential for transferase activity.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19903480 R.Banerjee, S.Chen, K.Dare, M.Gilreath, M.Praetorius-Ibba, M.Raina, N.M.Reynolds, T.Rogers, H.Roy, S.S.Yadavalli, and M.Ibba (2010).
tRNAs: cellular barcodes for amino acids.
  FEBS Lett, 584, 387-395.  
19720027 A.Bouhss, B.Al-Dabbagh, M.Vincent, B.Odaert, M.Aumont-Nicaise, P.Bressolier, M.Desmadril, D.Mengin-Lecreulx, M.C.Urdaci, and J.Gallay (2009).
Specific interactions of clausin, a new lantibiotic, with lipid precursors of the bacterial cell wall.
  Biophys J, 97, 1390-1397.  
19787708 H.Roy (2009).
Tuning the properties of the bacterial membrane with aminoacylated phosphatidylglycerol.
  IUBMB Life, 61, 940-953.  
19151092 M.Fonvielle, M.Chemama, R.Villet, M.Lecerf, A.Bouhss, J.M.Valéry, M.Ethève-Quelquejeu, and M.Arthur (2009).
Aminoacyl-tRNA recognition by the FemXWv transferase for bacterial cell wall synthesis.
  Nucleic Acids Res, 37, 1589-1601.  
18081839 A.Bouhss, A.E.Trunkfield, T.D.Bugg, and D.Mengin-Lecreulx (2008).
The biosynthesis of peptidoglycan lipid-linked intermediates.
  FEMS Microbiol Rev, 32, 208-233.  
18266857 J.L.Mainardi, R.Villet, T.D.Bugg, C.Mayer, and M.Arthur (2008).
Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria.
  FEMS Microbiol Rev, 32, 386-408.  
18451033 R.P.Garg, X.L.Qian, L.B.Alemany, S.Moran, and R.J.Parry (2008).
Investigations of valanimycin biosynthesis: elucidation of the role of seryl-tRNA.
  Proc Natl Acad Sci U S A, 105, 6543-6547.  
18063720 J.van Heijenoort (2007).
Lipid intermediates in the biosynthesis of bacterial peptidoglycan.
  Microbiol Mol Biol Rev, 71, 620-635.  
17932062 R.Villet, M.Fonvielle, P.Busca, M.Chemama, A.P.Maillard, J.E.Hugonnet, L.Dubost, A.Marie, N.Josseaume, S.Mesnage, C.Mayer, J.M.Valéry, M.Ethève-Quelquejeu, and M.Arthur (2007).
Idiosyncratic features in tRNAs participating in bacterial cell wall synthesis.
  Nucleic Acids Res, 35, 6870-6883.  
17242373 X.Dong, M.Kato-Murayama, T.Muramatsu, H.Mori, M.Shirouzu, Y.Bessho, and S.Yokoyama (2007).
The crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coli.
  Protein Sci, 16, 528-534.
PDB code: 2cxa
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.