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Crystallization and preliminary X-ray diffraction studies of the signal recognition particle receptor FtsY from Mycoplasma mycoides.
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Science and Technology).
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Science and Technology).
2000 (English)In: Acta Crystallogr D Biol Crystallogr, ISSN 0907-4449, Vol. 56, no Pt 8, 1030-2 p.Article in journal (Refereed) Published
Abstract [en]

The prokaryotic signal recognition particle (SRP) pathway comprises two proteins, Ffh and FtsY, homologous to the SRP54 and SRalpha proteins in the more complex eukaryotic system. All four proteins are part of a unique subfamily of GTPases. Four truncated versions of the 412 amino-acid FtsY receptor protein from Mycoplasma mycoides have been cloned, expressed in Escherichia coli and purified. Purified proteins from all constructs and the full-length FtsY protein were subjected to crystallization trials. Crystals were obtained for the construct which comprised residues 98-412 corresponding to the conserved NG-domain (residues 194-497 in E. coli). A native data set at 1.9 A resolution has been collected at 100 K using synchrotron radiation. The crystals belong to the space group P2(1)2(1)2, with unit-cell parameters a = 68.7, b = 101.1, c = 42.5 A and one molecule in the asymmetric unit.

Place, publisher, year, edition, pages
2000. Vol. 56, no Pt 8, 1030-2 p.
Keyword [en]
Bacterial Proteins/*chemistry/genetics, Base Sequence, Crystallization, Crystallography; X-Ray, DNA Primers/genetics, Escherichia coli/genetics, Mycoplasma mycoides/*chemistry/genetics, Receptors; Cytoplasmic and Nuclear/*chemistry/genetics, Recombinant Proteins/chemistry/genetics, Signal Recognition Particle/chemistry/genetics
Identifiers
URN: urn:nbn:se:umu:diva-13964PubMedID: 10944345OAI: oai:DiVA.org:umu-13964DiVA: diva2:153635
Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2011-01-14Bibliographically approved

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Sauer-Eriksson, Elisabeth

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