Structural characterization of a novel autonomous cohesin from Ruminococcus flavefaciens.
Ruminococcus flavefaciens is a cellulolytic bacterium found in the rumen of herbivores and produces one of the most elaborate and variable cellulosome systems. The structure of an R. flavefaciens protein (RfCohG, ZP_06142108), representing a freestanding (non-cellulosomal) type III cohesin module, has been determined. A selenomethionine derivative with a C-terminal histidine tag was crystallized and diffraction data were measured to 2.44 Å resolution. Its structure was determined by single-wavelength anomalous dispersion, revealing eight molecules in the asymmetric unit. RfCohG exhibits the most complex among all known cohesin structures, possessing four α-helical elements and a topographical protuberance on the putative dockerin-binding surface.
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel.
Milana
M
Voronov-Goldman
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel.
Maly
M
Levy-Assaraf
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel.
Oren
O
Yaniv
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel.
Gloria
G
Wisserman
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel.
Sadanari
S
Jindou
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel.
Ilya
I
Borovok
Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel.
Edward A
EA
Bayer
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel.
Raphael
R
Lamed
Department of Chemical Research Support, The Weizmann Institute of Science, Rehovot 76100, Israel.
Linda J W
LJ
Shimon
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel.
Felix
F
Frolow
D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism; D044603:Cellulosomes / Q000737:chemistry* / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D045857:Ruminococcus / Q000378:metabolism*; D012645:Selenomethionine / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014443:Tyrosine / Q000737:chemistry; D000097722:Cohesins
D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D012645:Selenomethionine; D014443:Tyrosine; D000097722:Cohesins
cellulose degradation; cellulosome; cohesin-dockerin interaction; glycoside hydrolases; scaffoldin