1JAW

AMINOPEPTIDASE P FROM E. COLI LOW PH FORM

Summary for 1JAW

• Entry DOI: 10.2210/pdb1jaw/pdb
• Descriptor: AMINOPEPTIDASE P, MANGANESE (II) ION, ACETATE ION, ... (4 entities in total)
• Functional Keywords: proline peptidase, hydrolase, aminopeptidase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P15034
• Total number of polymer chains: 1
• Total formula weight: 49928.98

Authors

Wilce, M.C.J.,Bond, C.S.,Lilley, P.E.,Dixon, N.E.,Freeman, H.C.,Guss, J.M. (deposition date: 1997-12-22, release date: 1999-04-06, Last modification date: 2024-02-07)

Primary citation

Wilce, M.C.,Bond, C.S.,Dixon, N.E.,Freeman, H.C.,Guss, J.M.,Lilley, P.E.,Wilce, J.A.
Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli.
Proc.Natl.Acad.Sci.USA, 95:3472-3477, 1998

PubMed Abstract: 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 physiological conditions. The monomer folds into two domains. The active site, in the larger C-terminal domain, contains a dinuclear manganese center in which a bridging water molecule or hydroxide ion appears poised to act as the nucleophile in the attack on the scissile peptide bond of Xaa-Pro. The metal-binding residues are located in a single subunit, but the residues surrounding the active site are contributed by three subunits. The fold of the protein resembles that of creatine amidinohydrolase (creatinase, not a metalloenzyme). The C-terminal catalytic domain is also similar to the single-domain enzyme methionine aminopeptidase that has a dinuclear cobalt center.

PubMed: 9520390
DOI: 10.1073/pnas.95.7.3472

Experimental method

X-RAY DIFFRACTION (2.7 Å)