Filamin C 23-24 (protein), FilaminC 23-24, Escherichia coli
Biological species
Escherichia coli (E. coli)
Citation
Journal: J Mol Biol / Year: 2007 Title: Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer. Authors: Ljiljana Sjekloća / Regina Pudas / Björn Sjöblom / Peter Konarev / Oliviero Carugo / Vladimir Rybin / Tiila-Riikka Kiema / Dmitri Svergun / Jari Ylänne / Kristina Djinović Carugo / Abstract: Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ...Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ultracentrifugation experiments on the constructs containing carboxy-terminal domains of the protein (domains 23-24 and 19-21). The crystal structure of domain 23 of filamin C showed that the protein adopts the expected immunoglobulin (Ig)-like fold. Small-angle X-ray scattering experiments performed on filamin C tandem Ig-like domains 23 and 24 reveal a dimer that is formed by domain 24 and that domain 23 has little interactions with itself or with domain 24, while the analytical ultracentrifugation experiments showed that the filamin C domains 19-21 form elongated monomers in diluted solutions.
Contact author
Petr Konarev (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)
Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron
Detector
Name: MAR 345 Image Plate
Scan
Title: Filamin C 23-24 / Measurement date: Jun 17, 2005 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 120 sec. / Number of frames: 2 / Unit: 1/nm /
Min
Max
Q
0.1893
4.5815
Distance distribution function P(R)
Sofotware P(R): GNOM 4.5a / Number of points: 480 /
Min
Max
Q
0.1916
4.581
P(R) point
10
489
R
0
13
Result
Type of curve: merged /
Experimental
Porod
MW
42 kDa
-
Volume
-
75 nm3
P(R)
Guinier
Forward scattering, I0
121
122
Radius of gyration, Rg
3.53 nm
3.5 nm
Min
Max
D
-
13
Guinier point
1
25
+
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