1zat
From Proteopedia
(New page: 200px<br /><applet load="1zat" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zat, resolution 2.40Å" /> '''Crystal Structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1zat.gif|left|200px]]<br /><applet load="1zat" size=" | + | [[Image:1zat.gif|left|200px]]<br /><applet load="1zat" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zat, resolution 2.40Å" /> | caption="1zat, resolution 2.40Å" /> | ||
'''Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution'''<br /> | '''Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | During the final stages of cell-wall synthesis in bacteria, penicillin-binding proteins (PBPs) catalyse the cross-linking of peptide | + | During the final stages of cell-wall synthesis in bacteria, penicillin-binding proteins (PBPs) catalyse the cross-linking of peptide chains from adjacent glycan strands of nascent peptidoglycan. We have recently shown that this step can be bypassed by an L,D-transpeptidase, which confers high-level beta-lactam-resistance in Enterococcus faecium. The resistance bypass leads to replacement of D-Ala4-->D-Asx-L-Lys3 cross-links generated by the PBPs by L-Lys3-->D-Asx-L-Lys3 cross-links generated by the L,D-transpeptidase. As the first structure of a member of this new transpeptidase family, we have determined the crystal structure of a fragment of the L,D-transpeptidase from E.faecium (Ldt(fm217)) at 2.4A resolution. Ldt(fm217) consists of two domains, the N-terminal domain, a new mixed alpha-beta fold, and the ErfK_YbiS_YhnG C-terminal domain, a representative of the mainly beta class of protein structures. Residue Cys442 of the C-terminal domain has been proposed to be the catalytic residue implicated in the cleavage of the L-Lys-D-Ala peptide bond. Surface analysis of Ldt(fm217) reveals that residue Cys442 is localized in a buried pocket and is accessible by two paths on different sides of the protein. We propose that the two paths to the catalytic residue Cys442 are the binding sites for the acceptor and donor substrates of the L,D-transpeptidase. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium] with ZN and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1ZAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAT OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 16: | ||
[[Category: Biarrotte-Sorin, S.]] | [[Category: Biarrotte-Sorin, S.]] | ||
[[Category: Gutmann, L.]] | [[Category: Gutmann, L.]] | ||
| - | [[Category: Hugonnet, J | + | [[Category: Hugonnet, J E.]] |
| - | [[Category: Mainardi, J | + | [[Category: Mainardi, J L.]] |
[[Category: Mayer, C.]] | [[Category: Mayer, C.]] | ||
[[Category: Rice, L.]] | [[Category: Rice, L.]] | ||
| Line 28: | Line 28: | ||
[[Category: peptidoglycan]] | [[Category: peptidoglycan]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:45 2008'' |
Revision as of 14:13, 21 February 2008
|
Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution
Overview
During the final stages of cell-wall synthesis in bacteria, penicillin-binding proteins (PBPs) catalyse the cross-linking of peptide chains from adjacent glycan strands of nascent peptidoglycan. We have recently shown that this step can be bypassed by an L,D-transpeptidase, which confers high-level beta-lactam-resistance in Enterococcus faecium. The resistance bypass leads to replacement of D-Ala4-->D-Asx-L-Lys3 cross-links generated by the PBPs by L-Lys3-->D-Asx-L-Lys3 cross-links generated by the L,D-transpeptidase. As the first structure of a member of this new transpeptidase family, we have determined the crystal structure of a fragment of the L,D-transpeptidase from E.faecium (Ldt(fm217)) at 2.4A resolution. Ldt(fm217) consists of two domains, the N-terminal domain, a new mixed alpha-beta fold, and the ErfK_YbiS_YhnG C-terminal domain, a representative of the mainly beta class of protein structures. Residue Cys442 of the C-terminal domain has been proposed to be the catalytic residue implicated in the cleavage of the L-Lys-D-Ala peptide bond. Surface analysis of Ldt(fm217) reveals that residue Cys442 is localized in a buried pocket and is accessible by two paths on different sides of the protein. We propose that the two paths to the catalytic residue Cys442 are the binding sites for the acceptor and donor substrates of the L,D-transpeptidase.
About this Structure
1ZAT is a Single protein structure of sequence from Enterococcus faecium with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a novel beta-lactam-insensitive peptidoglycan transpeptidase., Biarrotte-Sorin S, Hugonnet JE, Delfosse V, Mainardi JL, Gutmann L, Arthur M, Mayer C, J Mol Biol. 2006 Jun 9;359(3):533-8. Epub 2006 Mar 23. PMID:16647082
Page seeded by OCA on Thu Feb 21 16:13:45 2008
