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

Abstract：

: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 autocatalytic hydrolysis of the peptide bond between the C-terminal residue of the spacer and the active-site serine residue at the N terminus of the B chain. We have determined the crystal structure of a slowly processing precursor mutant (Thr263Gly) of penicillin G acylase from Escherichia coli, which reveals that the spacer peptide blocks the entrance to the active-site cleft consistent with an autocatalytic mechanism of maturation. In this mutant precursor there is, however, an unexpected cleavage at a site four residues from the active-site serine residue. Analyses of the stereochemistry of the 260-261 bond seen to be cleaved in this precursor structure and of the 263-264 peptide bond have suggested factors that may govern the autocatalytic mechanism.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Hewitt L,Kasche V,Lummer K,Lewis RJ,Murshudov GN,Verma CS,Dodson GG,Wilson KS

doi

10.1006/jmbi.2000.4105

keywords:

subject

Has Abstract

pub_date

2000-09-29 00:00:00

pages

887-98

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(00)94105-6

journal_volume

302

pub_type

杂志文章

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