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2ek8

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Revision as of 07:50, 26 March 2008


PDB ID 2ek8

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites: , , , , , and
Ligands: ,
Domains: Peptidase_M28, PA_C5a_like
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



Aminopeptidase from Aneurinibacillus sp. strain AM-1


Overview

To elucidate the structure and molecular mechanism of a characteristic proline-specific aminopeptidase produced by the thermophile Aneurinibacillus sp. strain AM-1, its gene was cloned and the recombinant protein was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 1.8 A resolution from the recombinant aminopeptidase crystal. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 93.62, b = 68.20, c = 76.84 A. A complete data set was also obtained from crystals of SeMet-substituted aminopeptidase. Data in the resolution range 20-2.1 A from the MAD data set from the SeMet-substituted crystal were used for phase determination.

About this Structure

2EK8 is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.

Reference

Overexpression, purification, crystallization and preliminary X-ray crystallographic studies of a proline-specific aminopeptidase from Aneurinibacillus sp. strain AM-1., Akioka M, Nakano H, Horikiri A, Tsujimoto Y, Matsui H, Shimizu T, Nakatsu T, Kato H, Watanabe K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1266-8. Epub 2006 Nov 30. PMID:17142913

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