Sandbox Reserved 1499

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===Structure of the active site===
===Structure of the active site===
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<scene name='80/802673/Active_site_1/1'>active site</scene>
===The role of pentapeptidic imitation by ampicillin===
===The role of pentapeptidic imitation by ampicillin===
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<scene name='80/802673/Active_site_amp/1'>ampicillin inserts into the active site</scene>

Revision as of 19:32, 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

3ita, resolution 1.80Å

Drag the structure with the mouse to rotate

Relevance

The resolution of this structure played an important role in understanding the method of action of beta-lactam antibiotics.[3]

References

  1. ↑ Chen Y, Zhang W, Shi Q, Hesek D, Lee M, Mobashery S, Shoichet BK. Crystal structures of penicillin-binding protein 6 from Escherichia coli. J Am Chem Soc. 2009 Oct 14;131(40):14345-54. PMID:19807181 doi:10.1021/ja903773f
  2. ↑ Mattei PJ, Neves D, Dessen A. Bridging cell wall biosynthesis and bacterial morphogenesis. Curr Opin Struct Biol. 2010 Dec;20(6):749-55. doi: 10.1016/j.sbi.2010.09.014., Epub 2010 Oct 26. PMID:21030247 doi:http://dx.doi.org/10.1016/j.sbi.2010.09.014
  3. ↑ Llarrull LI, Testero SA, Fisher JF, Mobashery S. The future of the beta-lactams. Curr Opin Microbiol. 2010 Oct;13(5):551-7. doi: 10.1016/j.mib.2010.09.008. Epub, 2010 Sep 29. PMID:20888287 doi:http://dx.doi.org/10.1016/j.mib.2010.09.008
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