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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. | ||
[[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 == |
<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=''> | ||
| - | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| - | + | [[3ita]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ITA OCA]. | |
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== Relevance == | == Relevance == | ||
| - | == Publication Abstract from PubMed == | ||
| - | Penicillin-binding protein 6 (PBP6) is one of the two main DD-carboxypeptidases in Escherichia coli, which are implicated in maturation of bacterial cell wall and formation of cell shape. Here, we report the first X-ray crystal structures of PBP6, capturing its apo state (2.1 A), an acyl-enzyme intermediate with the antibiotic ampicillin (1.8 A), and for the first time for a PBP, a preacylation complex (a "Michaelis complex", determined at 1.8 A) with a peptidoglycan substrate fragment containing the full pentapeptide, NAM-(L-Ala-D-isoGlu-L-Lys-D-Ala-D-Ala). These structures illuminate the molecular interactions essential for ligand recognition and catalysis by DD-carboxypeptidases, and suggest a coupling of conformational flexibility of active site loops to the reaction coordinate. The substrate fragment complex structure, in particular, provides templates for models of cell wall recognition by PBPs, as well as substantiating evidence for the molecular mimicry by beta-lactam antibiotics of the peptidoglycan acyl-D-Ala-D-Ala moiety. | ||
Crystal structures of penicillin-binding protein 6 from Escherichia coli.,Chen Y, Zhang W, Shi Q, Hesek D, Lee M, Mobashery S, Shoichet BK J Am Chem Soc. 2009 Oct 14;131(40):14345-54. PMID:19807181<ref>PMID:19807181</ref> | Crystal structures of penicillin-binding protein 6 from Escherichia coli.,Chen Y, Zhang W, Shi Q, Hesek D, Lee M, Mobashery S, Shoichet BK J Am Chem Soc. 2009 Oct 14;131(40):14345-54. PMID:19807181<ref>PMID:19807181</ref> | ||
Revision as of 16:28, 10 January 2019
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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.
Structure
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