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

TitleCrystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate.
Publication TypeJournal Article
Year of Publication2005
AuthorsPauwels, K., R. Loris, G. Vandenbussche, J. Marie Ruysschaert, L. Wyns, and P. Van Gelder
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume61
IssuePt 8
Pagination791-5
Date Published2005 Aug 1
ISSN1744-3091
KeywordsBacterial Proteins, 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.

DOI10.1107/S1744309105023055
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID16511160
PubMed Central IDPMC1952342