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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 --> | ||
| + | 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=''> | ||
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<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. |
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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. 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
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