This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox Reserved 1499
From Proteopedia
m |
m |
||
| Line 1: | Line 1: | ||
{{Sandbox_Reserved_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| + | 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. Here, its structure is shown 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. | ||
| + | [[http://www.uniprot.org/uniprot/DACC_ECOLI DACC_ECOLI]] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | ||
== Structural highlights == | == Structural highlights == | ||
<StructureSection load='3ita' size='340' side='right' caption='[[3ita]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3ita' size='340' side='right' caption='[[3ita]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| Line 12: | Line 16: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ita FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ita OCA], [http://pdbe.org/3ita PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ita RCSB], [http://www.ebi.ac.uk/pdbsum/3ita PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ita ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ita FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ita OCA], [http://pdbe.org/3ita PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ita RCSB], [http://www.ebi.ac.uk/pdbsum/3ita PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ita ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/DACC_ECOLI DACC_ECOLI]] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:21, 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:
More help: Help:Editing |
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. Here, its structure is shown 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.
Structural highlights
| |||||||||||
