1a16

File:1a16.gif

spinqualitylabelsall models 1a16, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU

OverviewOverview

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.

About this StructureAbout this Structure

1A16 is a Single protein structure of sequence from Escherichia coli with MN as ligand. Active as Xaa-Pro aminopeptidase, with EC number 3.4.11.9 Structure known Active Site: NUL. Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli., Wilce MC, Bond CS, Dixon NE, Freeman HC, Guss JM, Lilley PE, Wilce JA, Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3472-7. PMID:9520390

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