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Crystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate

Publication Type:

Journal Article

Authors:

Pauwels,K.; Loris,R.; Vandenbussche,G.; Ruysschaert,J.M.; Wyns,L.; Van,Gelder P.

Source:

Volume 61, Issue Pt 8, p.791 - 795 (2005)

URL:

PM:16511160

Keywords:

Bacterial Proteins; chemistry; Burkholderia; Crystallization; Electrophoresis; Polyacrylamide Gel; Lipase; Molecular Chaperones; X-Ray Diffraction

Abstract:

Bacterial lipases that are secreted via the type II secretion pathway require a lipase-specific foldase in order to obtain their native and biologically active conformation in the periplasmic space. The lipase-foldase complex from Burkholderia glumae (319 and 333 residues, respectively) was crystallized in two crystal forms. One crystal form belongs to space group P3(1)21 (P3(2)21), with unit-cell parameters a = b = 122.3, c = 98.2 A. A procedure is presented which improved the diffraction of these crystals from approximately 5 to 2.95 A. For the second crystal form, which belonged to space group C2 with unit-cell parameters a = 183.0, b = 75.7, c = 116.6 A, X-ray data were collected to 1.85 A

Notes:

DA - 20060302
IS - 1744-3091 (Electronic)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Bacterial Proteins)
RN - 0 (Molecular Chaperones)
RN - EC 3.1.1.3 (Lipase)
RN - EC 3.1.1.3 (lipase foldase)
SB - IM