2dq6

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File:2dq6.gif


2dq6, resolution 1.50Å

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Crystal Structure of Aminopeptidase N from Escherichia coli

OverviewOverview

Aminopeptidase N from Escherichia coli is a broad specificity zinc, exopeptidase belonging to aminopeptidase clan MA, family M1. The, structures of the ligand-free form and the enzyme-bestatin complex were, determined at 1.5- and 1.6-A resolution, respectively. The enzyme is, composed of four domains: an N-terminal beta-domain (Met(1)-Asp(193)), a, catalytic domain (Phe(194)-Gly(444)), a middle beta-domain, (Thr(445)-Trp(546)), and a C-terminal alpha-domain (Ser(547)-Ala(870))., The structure of the catalytic domain exhibits similarity to thermolysin, and a metal-binding motif (HEXXHX(18)E) is found in the domain. The zinc, ion is coordinated by His(297), His(301), Glu(320), and a water molecule., The groove on the catalytic domain that contains the active site is, covered by the C-terminal alpha-domain, and a large cavity is formed, inside the protein. However, there exists a small hole at the center of, the C-terminal alpha-domain. The N terminus of bestatin is recognized by, Glu(121) and Glu(264), which are located in the N-terminal and catalytic, domains, respectively. Glu(298) and Tyr(381), located near the zinc ion, are considered to be involved in peptide cleavage. A difference revealed, between the ligand-free form and the enzyme-bestatin complex indicated, that Met(260) functions as a cushion to accept substrates with different, N-terminal residue sizes, resulting in the broad substrate specificity of, this enzyme.

About this StructureAbout this Structure

2DQ6 is a Single protein structure of sequence from Escherichia coli with ZN and SO4 as ligands. Active as Membrane alanyl aminopeptidase, with EC number 3.4.11.2 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition., Ito K, Nakajima Y, Onohara Y, Takeo M, Nakashima K, Matsubara F, Ito T, Yoshimoto T, J Biol Chem. 2006 Nov 3;281(44):33664-76. Epub 2006 Aug 2. PMID:16885166

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