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1XF8

Crystal Structure of Weissella viridescens FemX (Y254F) Mutant

Summary for 1XF8
Entry DOI10.2210/pdb1xf8/pdb
Related1LRZ 1NE9 1P4N 1XE4
DescriptorFemX, MAGNESIUM ION (3 entities in total)
Functional Keywordsmutant, femx, ligase, transferase
Biological sourceWeissella viridescens
Total number of polymer chains1
Total formula weight38204.11
Authors
Biarrotte-Sorin, S.,Maillard, A.P.,Arthur, M.,Mayer, C. (deposition date: 2004-09-14, release date: 2005-05-31, Last modification date: 2023-10-25)
Primary citationMaillard, A.P.,Biarrotte-Sorin, S.,Villet, R.,Mesnage, S.,Bouhss, A.,Sougakoff, W.,Mayer, C.,Arthur, M.
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, 2005
Cited by
PubMed Abstract: 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.
PubMed: 15901708
DOI: 10.1128/JB.187.11.3833-3838.2005
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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数据于2024-11-06公开中

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