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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 is shown 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>. [[3ita]] shows its structure as an acyl-enzyme complex with ampicillin.
== 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.

Revision as of 16:38, 10 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.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

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]. 3ita shows its structure as an acyl-enzyme complex with ampicillin.

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. [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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