SASDAE4: C-terminal CtBP3 (C-term part CtBP3, C-term CtBP3)

Basic information

• Entry: Database: SASBDB / ID: SASDAE4

Sample

C-terminal CtBP3

• C-term part CtBP3 (protein), C-term CtBP3

• Citation: Journal: Protein Sci / Year: 2006; Title: The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured.; Authors: Marco Nardini / Dmitri Svergun / Peter V Konarev / Stefania Spanò / Mauro Fasano / Chiara Bracco / Alessandra Pesce / Alessandra Donadini / Claudia Cericola / Francesco Secundo / Alberto Luini / Daniela Corda / Martino Bolognesi / ; Abstract: C-terminal binding proteins (CtBPs) are moonlighting proteins involved in nuclear transcriptional corepression and in Golgi membrane tubule fission. Structural information on CtBPs is available for their substrate-binding domain, responsible for transcriptional repressor recognition/binding, and for the nucleotide-binding domain, involved in NAD(H)-binding and dimerization. On the contrary, little is known about the structure of CtBP C-terminal region ( approximately 90 residues), hosting sites for post-translational modifications. In the present communication we apply a combined approach based on bioinformatics, nuclear magnetic resonance, circular dichroism spectroscopy, and small-angle X-ray scattering, and we show that the CtBP C-terminal region is intrinsically unstructured in the full-length CtBP and in constructs lacking the substrate- and/or the nucleotide-binding domains. The flexible nature of this protein region, and its structural transitions, may be instrumental for CtBP recognition and binding to diverse molecular partners.

Contact author

• Petr Konarev (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

Models

• Model #59: ; Type: dummy / Software: Dammin / Symmetry: P2 / Chi-square value: 3.2041; Search similar-shape structures of this assembly by Omokage search (details)
• Model #60: ; Type: mix / Software: Bunch / Radius of dummy atoms: 1.90 A / Comment: P2 / Chi-square value: 2.4025; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: C-terminal CtBP3 / Sample MW: 52 kDa / Specimen concentration: 2.00-8.00
• Buffer: Name: 25 mM Tris/HCl / pH: 8 / Composition: 250 mM NaCl

Entity #54

Name: C-term CtBP3 / Type: protein / Description: C-term part CtBP3 / Formula weight: 26.5 / Num. of mol.: 2
Sequence:

HHHHHHMSGV RPPIMNGPMH PRPLVALLDG RDTVEMPILK DVATVAFCDA QSTQEIHEKV LNEAVGALMY HTITLTREDL EKFKALRIIV RIGSGFDNID IKSAGDLGIA VCNVPAASGS SWYSEQASIE MREEAAREIR RAITGRIPDS LKNCVNKDHL TAATHWASMD PAVVHPELNG AAYSRYPPGV VSVAPTGIPA AVEGIVPSAM SLSHGLPPVA HPPHAPSPGQ TVKPEADRDH TTDQL

Experimental information

• Beam: Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron
• Detector: Name: MAR 345 Image Plate

Scan

Title: C-terminal part CtBP3 / Measurement date: Nov 18, 2004 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 120 sec. / Number of frames: 2 / Unit: 1/nm /

	Min	Max
Q	0.1608	4.485

Distance distribution function P(R)

Sofotware P(R): GNOM 4.5a / Number of points: 498 /

	Min	Max
Q	0.1411	4.483
P(R) point	1	498
R	0	20

Result

Type of curve: single_conc /

	Experimental	Porod
MW	56 kDa	-
Volume	-	126 nm3

	P(R)	Guinier
Forward scattering, I0	101	10500
Radius of gyration, Rg	5.6 nm	5.5 nm

	Min	Max
D	-	20
Guinier point	1	18