Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft
- 29 September 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 302 (4) , 887-898
- https://doi.org/10.1006/jmbi.2000.4105
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Ligand-induced conformational change in penicillin acylaseJournal of Molecular Biology, 1998
- Conformational constraints for protein self-cleavage in the proteasomeJournal of Molecular Biology, 1998
- An extensively modified version of MolScript that includes greatly enhanced coloring capabilitiesJournal of Molecular Graphics and Modelling, 1997
- A protein catalytic framework with an N-terminal nucleophile is capable of self-activationNature, 1995
- The prosegment–subtilisin BPN′ complex: crystal structure of a specific ‘foldase’Structure, 1995
- Penicillin acylase has a single-amino-acid catalytic centreNature, 1995
- Molecular biology of ?-lactam acylasesWorld Journal of Microbiology and Biotechnology, 1994
- Effects of site-directed mutations on processing and activities of penicillin G acylase from Escherichia coli ATCC 11105Journal of Bacteriology, 1992
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Geometrical reaction coordinates. II. Nucleophilic addition to a carbonyl groupJournal of the American Chemical Society, 1973