Sandbox Reserved 1499

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 11: Line 11:
[[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='80/802673/3ita_full/1'>
+
<StructureSection load='3ita' size='340' side='right' caption='[[3ita]], [[Resolution|resolution]] 1.80&Aring;' scene='80/802673/Default/1'>
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.
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.
- 
===Structure of the active site===
===Structure of the active site===
<scene name='80/802673/Active_site_1/1'>active site</scene>
<scene name='80/802673/Active_site_1/1'>active site</scene>
Line 19: Line 18:
===The role of pentapeptidic imitation by ampicillin===
===The role of pentapeptidic imitation by ampicillin===
<scene name='80/802673/Active_site_amp/1'>ampicillin inserts into the active site</scene>
<scene name='80/802673/Active_site_amp/1'>ampicillin inserts into the active site</scene>
-
 
+
<scene name='80/802673/Cat_water/2'>water</scene>
-
 
+
</StructureSection>
</StructureSection>
== Relevance ==
== Relevance ==

Revision as of 20:05, 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.
  • 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 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
Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1499"
Personal tools