title: Crystallization of a Golgi-associated PR-1-related protein (GAPR-1) that localizes to lipid-enriched microdomains.
abstract: The human Golgi-associated PR-1-related protein (GAPR-1) is closely related to plant pathogenesis-related (PR-1) proteins, which are upregulated in response to pathogen attack. Family members have been identified in a variety of organisms, together constituting the superfamily of PR-1 proteins. GAPR-1 is found within lipid-enriched microdomains on the cytosolic side of the endomembrane system. GAPR-1 is tightly anchored to membranes and absent from the cytosol, although it does not possess a membrane-spanning domain. Crystals of recombinantly expressed GAPR-1 have been grown that diffract to high (1.5 A) resolution. Complete data sets have been collected on a trigonal crystal form (P3(1)21/P3(2)21), with unit-cell parameters a = b = 73.5, c = 63.2 A. Molecular replacement using the NMR coordinates of tomato pathogenesis-related protein (28% identity) was unsuccessful and a search for heavy-metal derivatives or alternative phasing methods has been initiated.
authors.affiliation: Structural Biology Program, EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany. matthew.groves@embl-hamburg.de
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Groves
authors.forename: Audrey
authors.initials: A
authors.lastname: Kuhn
authors.forename: Astrid
authors.initials: A
authors.lastname: Hendricks
authors.forename: Susanne
authors.initials: S
authors.lastname: Radke
authors.forename: Ramon L
authors.initials: RL
authors.lastname: Serrano
authors.forename: J Bernd
authors.initials: JB
authors.lastname: Helms
authors.forename: Irmgard
authors.initials: I
authors.lastname: Sinning
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D021962:Membrane Microdomains / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*
chemical_list: C458481:GLIPR2 protein, human; D008565:Membrane Proteins