Ontology highlight
ABSTRACT:
SUBMITTER: Wilce MC
PROVIDER: S-EPMC19860 | biostudies-literature | 1998 Mar
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 19980301 7
The structure of the proline-specific aminopeptidase (EC 3.4.11.9) from Escherichia coli has been solved and refined for crystals of the native enzyme at a 2.0-A resolution, for a dipeptide-inhibited complex at 2.3-A resolution, and for a low-pH inactive form at 2.7-A resolution. The protein crystallizes as a tetramer, more correctly a dimer of dimers, at both high and low pH, consistent with observations from analytical ultracentrifuge studies that show that the protein is a tetramer under phys ...[more]