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Cloning, purification, crystallization and preliminary X‐ray diffraction studies of Escherichia coli PapD‐like protein (EcpD)
Author(s) -
Pandey Nishant Kumar,
Pal Ravi Kant,
Kashyap Maruthi,
Bhavesh Neel Sarovar
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112027364
Subject(s) - escherichia coli , periplasmic space , bacterial outer membrane , fimbria , biogenesis , pilus , biology , bacterial adhesin , chaperone (clinical) , virulence , intimin , microbiology and biotechnology , fimbriae proteins , flagellum , bacteria , crystallography , biophysics , biochemistry , chemistry , enterobacteriaceae , gene , genetics , medicine , pathology
Many Gram‐negative bacteria are characterized by hair‐like proteinaceous appendages on their surface known as fimbriae. In uropathogenic strains of Escherichia coli , fimbriae mediate attachment by binding to receptors on the host cell, often contributing to virulence and disease. E. coli PapD‐like protein (EcpD) is a periplasmic chaperone that plays an important role in the proper folding and guiding of Yad fimbrial proteins to the outer membrane usher protein in a process known as pilus biogenesis. EcpD is essential for pilus biogenesis in uropathogenic E. coli and plays an important role in virulence. In the present study, EcpD was cloned, overexpressed, purified and crystallized by the hanging‐drop vapour‐diffusion method. The crystals diffracted to 1.67 Å resolution and belonged to the orthorhombic space group C 222 1 , with unit‐cell parameters a = 100.3, b = 127.6, c = 45.9 Å. There was a single molecule in the asymmetric unit and the corresponding Matthews coefficient was calculated to be 3.02 Å 3  Da −1 , with 59% solvent content. Initial phases were determined by molecular replacement.

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