Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft.

doi:10.1006/jmbi.2000.4105

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Article

Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft.

Journal of molecular biology - 29 Sept 2000

Hewitt L, Kasche V, Lummer K, Lewis R J, Murshudov G N, Verma C S, Dodson G G, Wilson K S

Abstract excerpt

Penicillin G acylase is a periplasmic protein, cytoplasmically expressed as a precursor polypeptide comprising a signal sequence, the A and B chains of the mature enzyme (209 and 557 residues respectively) joined by a spacer peptide of 54 amino acid residues. The wild-type AB heterodimer is produced by proteolytic removal of this spacer in the periplasm. The first step in processing is believed to be...

Topics

Binding Sites
Catalysis
Crystallography, X-Ray
Electrons
Enzyme Precursors
Escherichia coli
Hydrogen Bonding
Hydrolases
Kinetics
Models, Molecular
Multigene Family

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Penicillin Amidase

Peptide Fragments

Protein Conformation

Protein Processing, Post-Translational

Protein Sorting Signals

Serine

Source

Open in PubMed

Identifiers

PMID: 10993730
DOI: 10.1006/jmbi.2000.4105

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