PMID:9520390
| Citation |
Wilce, MC, Bond, CS, Dixon, NE, Freeman, HC, Guss, JM, Lilley, PE and Wilce, JA (1998) Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 95:3472-7 |
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| 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. |
| Links | |
| Keywords |
Aminopeptidases/chemistry; Aminopeptidases/genetics; Aminopeptidases/metabolism; Binding Sites; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Molecular Sequence Data; Protein Conformation; Structure-Activity Relationship; Substrate Specificity |
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