Sandbox Reserved 1499
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{{Sandbox_Reserved_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | ==Penicillin-binding protein 6== | + | ==Penicillin-binding protein 6 from ''Escherichia coli''== |
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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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. | 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. | 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. | ||
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| - | Ampicillin <ref>DOI 10.1016/j.mib.2010.09.008</ref> | ||
[[http://www.uniprot.org/uniprot/DACC_ECOLI DACC_ECOLI]] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | [[http://www.uniprot.org/uniprot/DACC_ECOLI DACC_ECOLI]] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | ||
== Structure== | == Structure== | ||
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== Relevance == | == Relevance == | ||
| - | + | The role of beta-lactam antibiotics.<ref>DOI 10.1016/j.mib.2010.09.008</ref> | |
== References == | == References == | ||
Revision as of 12:41, 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 from Escherichia coli
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. [DACC_ECOLI] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Structure
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