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| {{STRUCTURE_1xe4| PDB=1xe4 | SCENE= }} | | {{STRUCTURE_1xe4| PDB=1xe4 | SCENE= }} |
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| '''Crystal Structure of Weissella viridescens FemX (K36M) Mutant'''
| | ===Crystal Structure of Weissella viridescens FemX (K36M) Mutant=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15901708}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15901708 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15901708}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ligase]] | | [[Category: Ligase]] |
| [[Category: Mutant]] | | [[Category: Mutant]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:54:42 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:41:30 2008'' |
