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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==
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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>. [[3ita]] shows its structure as an acyl-enzyme complex with ampicillin.
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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>.
<ref>DOI 10.1016/j.sbi.2010.09.014</ref>
<ref>DOI 10.1016/j.sbi.2010.09.014</ref>
== Function ==
== Function ==
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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. Ampicillin <ref>DOI 10.1016/j.mib.2010.09.008</ref>
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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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The cleavage reaction takes place in two step.
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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.
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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==
<StructureSection load='3ita' size='340' side='right' caption='[[3ita]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3ita' size='340' side='right' caption='[[3ita]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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The PBP6 is composed of 4 monomers which are almost identical to each other. The differences are found in some loops and in the amino acids of the active site.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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===Structure of the active site===
===Structure of the active site===

Revision as of 12:37, 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.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
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More help: Help:Editing

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]

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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