1xix
From Proteopedia
(New page: 200px<br /><applet load="1xix" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xix, resolution 2.00Å" /> '''Crystal Structure of...) |
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| - | [[Image:1xix.gif|left|200px]]<br /><applet load="1xix" size=" | + | [[Image:1xix.gif|left|200px]]<br /><applet load="1xix" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xix, resolution 2.00Å" /> | caption="1xix, resolution 2.00Å" /> | ||
'''Crystal Structure of Weissella viridescens FemX Form II'''<br /> | '''Crystal Structure of Weissella viridescens FemX Form II'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Weissella viridescens FemX (FemX(Wv)) belongs to the Fem family of | + | 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== | ==About this Structure== | ||
| - | 1XIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Weissella_viridescens Weissella viridescens]. Active as [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] Full crystallographic information is available from [http:// | + | 1XIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Weissella_viridescens Weissella viridescens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XIX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Arthur, M.]] | [[Category: Arthur, M.]] | ||
[[Category: Biarrotte-Sorin, S.]] | [[Category: Biarrotte-Sorin, S.]] | ||
| - | [[Category: Maillard, A | + | [[Category: Maillard, A P.]] |
[[Category: Mayer, C.]] | [[Category: Mayer, C.]] | ||
[[Category: crystal form ii]] | [[Category: crystal form ii]] | ||
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[[Category: ligase]] | [[Category: ligase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:26 2008'' |
Revision as of 13:55, 21 February 2008
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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. Active as UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase, with EC number 2.3.2.10 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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