1xix
From Proteopedia
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- | [[Image:1xix.gif|left|200px]] | + | [[Image:1xix.gif|left|200px]] |
- | + | ||
- | '''Crystal Structure of Weissella viridescens FemX Form II''' | + | {{Structure |
+ | |PDB= 1xix |SIZE=350|CAPTION= <scene name='initialview01'>1xix</scene>, resolution 2.00Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylmuramoylpentapeptide-lysine_N(6)-alanyltransferase UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.10 2.3.2.10] | ||
+ | |GENE= femx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1629 Weissella viridescens]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of Weissella viridescens FemX Form II''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1XIX is a [ | + | 1XIX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Weissella_viridescens Weissella viridescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XIX OCA]. |
==Reference== | ==Reference== | ||
- | Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens., Maillard AP, Biarrotte-Sorin S, Villet R, Mesnage S, Bouhss A, Sougakoff W, Mayer C, Arthur M, J Bacteriol. 2005 Jun;187(11):3833-8. PMID:[http:// | + | Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens., Maillard AP, Biarrotte-Sorin S, Villet R, Mesnage S, Bouhss A, Sougakoff W, Mayer C, Arthur M, J Bacteriol. 2005 Jun;187(11):3833-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15901708 15901708] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase]] | [[Category: UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase]] | ||
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[[Category: ligase]] | [[Category: ligase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:10:25 2008'' |
Revision as of 13:10, 20 March 2008
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, resolution 2.00Å | |||||||
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Gene: | femx (Weissella viridescens) | ||||||
Activity: | UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase, with EC number 2.3.2.10 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of Weissella viridescens FemX Form II
Overview
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.
About this Structure
1XIX is a Single protein structure of sequence from Weissella viridescens. Full crystallographic information is available from OCA.
Reference
Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens., Maillard AP, Biarrotte-Sorin S, Villet R, Mesnage S, Bouhss A, Sougakoff W, Mayer C, Arthur M, J Bacteriol. 2005 Jun;187(11):3833-8. PMID:15901708
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