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The Penicillin-binding protein 6 (PBP6) is a DD-carboxypeptidase from ''Escherichia coli'' which plays an important role in the creation of the bacterial cell wall. Its structure was determined by Chen et al.<ref>PMID:19807181</ref>.
The Penicillin-binding protein 6 (PBP6) is a DD-carboxypeptidase from ''Escherichia coli'' which plays an important role in the creation of the bacterial cell wall. Its structure was determined by Chen et al.<ref>PMID:19807181</ref>.
<ref>DOI 10.1016/j.sbi.2010.09.014</ref>
<ref>DOI 10.1016/j.sbi.2010.09.014</ref>
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== Function ==
== Function ==
As a DD-carboxypeptidase, the function of PBP6 is to participate in the transpeptidation which occurs during the biosynthesis of peptidoglycan. More specifically, it cleaves the peptide bond between the two terminal D-alanines of muramyl peptides. This then allows transpeptidases to create peptidoglycan cross-links which stabilise the cell wall.
As a DD-carboxypeptidase, the function of PBP6 is to participate in the transpeptidation which occurs during the biosynthesis of peptidoglycan. More specifically, it cleaves the peptide bond between the two terminal D-alanines of muramyl peptides. This then allows transpeptidases to create peptidoglycan cross-links which stabilise the cell wall.
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>

Revision as of 12:39, 11 January 2019

This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.
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Penicillin-binding protein 6

The Penicillin-binding protein 6 (PBP6) is a DD-carboxypeptidase from Escherichia coli which plays an important role in the creation of the bacterial cell wall. Its structure was determined by Chen et al.[1]. [2]

Contents

Function

As a DD-carboxypeptidase, the function of PBP6 is to participate in the transpeptidation which occurs during the biosynthesis of peptidoglycan. More specifically, it cleaves the peptide bond between the two terminal D-alanines of muramyl peptides. This then allows transpeptidases to create peptidoglycan cross-links which stabilise the cell wall. The cleavage reaction takes place in two step. Firstly, the PBP6 binds to carbonyl group in the peptide bond between the two terminal D-alanines of the N-acetylmuramic acid. This forms a high-energy tetrahedric intermediate called the acylenzyme. 3ita shows the acylenzyme complex of PBP6 with ampicillin. The acylenzyme allows the medium to reach the carbonyle group. As a result, a water molecule can attack the group, causing the cleavage of the tetrahedral structure.

Ampicillin [3] [DACC_ECOLI] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.

Structure

3ita, resolution 1.80Å

Drag the structure with the mouse to rotate
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