PMID: 9188744Jun 1, 1997Paper

Expression, crystallization and preliminary X-ray diffraction study of FtsY, the docking protein of the signal recognition particle of E. coli

Proteins
G MontoyaI Sinning

Abstract

FtsY is the docking protein or SR alpha homologue in E. coli. It is involved in targeting secretory proteins to the cytoplasmic membrane by interacting with the signal recognition particle, controlled by guanosine 5'-triphosphate. Two different constructs have been used in crystallization studies: the full-length protein and a truncated fragment with a his-tag at the C terminus. Only the second construct resulted in crystals suitable for x-ray diffraction. The crystals belong to the monoclinic space group P2(1) with cell dimensions a = 32.20 A, b = 79.57 A, c = 59.21 A, and beta = 94.45, and contain one molecule per asymmetric unit. At cryogenic temperatures the crystals diffract to a resolution limit of 2.5 A by using a rotating anode, and beyond 1.8 A by using synchrotron radiation.

References

Apr 1, 1990·Molecular Microbiology·D R Gill, G P Salmond
Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Mar 15, 1995·European Journal of Biochemistry·H Lütcke
Mar 1, 1993·Microbiological Reviews·A P Pugsley
Jan 1, 1994·Molecular Microbiology·J Luirink, B Dobberstein

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Citations

Oct 23, 1997·Proceedings of the National Academy of Sciences of the United States of America·C MoserI Sinning
May 6, 2011·The Journal of Biological Chemistry·Goran StjepanovicIrmgard Sinning
Sep 3, 2011·Microbiology and Molecular Biology Reviews : MMBR·Natalie VerstraetenJan Michiels
Feb 13, 2013·The Journal of Cell Biology·David AkopianShu-ou Shan
Dec 14, 2005·Journal of Structural Biology·Talal GarianiA Elisabeth Sauer-Eriksson
Dec 31, 1997·FEBS Letters·E de LeeuwJ Luirink
Oct 28, 2003·The Journal of Biological Chemistry·Martin van der LaanArnold J M Driessen
Nov 16, 2004·The Journal of Biological Chemistry·Barbara ZambelliStefano Ciurli
Jun 19, 2009·Current Microbiology·Hui-Jun DongYong-Quan Li

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