SASDCL7: Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-390)

Basic information

• Entry: Database: SASBDB / ID: SASDCL7

Sample

Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-390)

• Cytohesin-3 (protein), Cyth3, Mus musculus

Function / homology

Function:

Intra-Golgi traffic / Golgi vesicle transport / establishment of epithelial cell polarity / regulation of ARF protein signal transduction / phosphatidylinositol-3,4,5-trisphosphate binding / positive regulation of cell adhesion / bicellular tight junction / ruffle / guanyl-nucleotide exchange factor activity / adherens junction / nucleoplasm / plasma membrane / cytoplasm / cytosol

Domain/homology:

Sec7 domain / Sec7, C-terminal domain superfamily / Sec7 domain superfamily / Sec7 domain / SEC7 domain profile. / Sec7 domain / PH domain / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / PH-like domain superfamily

Component:

Cytohesin-3

• Biological species: Mus musculus (house mouse)
• Citation: Journal: Structure / Year: 2018; Title: Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors.; Authors: Andrew W Malaby / Sanchaita Das / Srinivas Chakravarthy / Thomas C Irving / Osman Bilsel / David G Lambright / ; Abstract: Membrane dynamic processes including vesicle biogenesis depend on Arf guanosine triphosphatase (GTPase) activation by guanine nucleotide exchange factors (GEFs) containing a catalytic Sec7 domain and a membrane-targeting module such as a pleckstrin homology (PH) domain. The catalytic output of cytohesin family Arf GEFs is controlled by autoinhibitory interactions that impede accessibility of the exchange site in the Sec7 domain. These restraints can be relieved through activator Arf-GTP binding to an allosteric site comprising the PH domain and proximal autoinhibitory elements (Sec7-PH linker and C-terminal helix). Small-angle X-ray scattering and negative-stain electron microscopy were used to investigate the structural organization and conformational dynamics of cytohesin-3 (Grp1) in autoinhibited and active states. The results support a model in which hinge dynamics in the autoinhibited state expose the activator site for Arf-GTP binding, while subsequent C-terminal helix unlatching and repositioning unleash conformational entropy in the Sec7-PH linker to drive exposure of the exchange site.

Contact author

• David Lambright (UMASS Medical School)

Models

• Model #1550: ; Type: mix / Software: (CORAL05) / Symmetry: P1; Comment: Sec7 and PH domains derived from 2R09; MSE converted to MET; Chi-square value: 1.24 / P-value: 0.003800; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1551: ; Type: mix / Software: (2.1) / Symmetry: P1; Comment: Sec7 and PH domains derived from 2R09; MSE converted to MET; Chi-square value: 1.079 / P-value: 0.004000; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1552: ; Type: mix / Software: (2.1) / Symmetry: P1; Comment: Sec7 and PH domains derived from 2R09; MSE converted to MET; Chi-square value: 1.079 / P-value: 0.004000; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1553: ; Type: mix / Software: (2.1) / Symmetry: P1; Comment: Sec7 and PH domains derived from 2R09; MSE converted to MET; Chi-square value: 1.079 / P-value: 0.004000; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1554: ; Type: dummy / Software: (r2835) / Radius of dummy atoms: 2.00 A / Symmetry: P1 / Comment: Most representative of 100 dammif models / Chi-square value: 2.579236 / P-value: 0.000960; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1555: ; Type: dummy / Radius of dummy atoms: 2.25 A / Symmetry: P1; Comment: Filtered average of 10 filtered averages of 10 dammif models; Chi-square value: 2.579236 / P-value: 0.000960; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-390); Specimen concentration: 2 mg/ml
• Buffer: Name: 20 mM Tris, 150 mM NaCl, 2 mM MgCl2, 0.001 mM inositol 1,3,4,5-tetrakisphosphate; pH: 8

Entity #790

Name: Cyth3 / Type: protein / Description: Cytohesin-3 / Formula weight: 40.355 / Num. of mol.: 1 / Source: Mus musculus / References: UniProt: O08967
Sequence:

MGHHHHHHGS TTQRNAQIAM GRKKFNMDPK KGIQFLIEND LLQSSPEDVA QFLYKGEGLN KTVIGDYLGE RDDFNIKVLQ AFVELHEFAD LNLVQALRQF LWSFRLPGEA QKIDRMMEAF ASRYCLCNPG VFQSTDTCYV LSFAIIMLNT SLHNHNVRDK PTAERFITMN RGINEGGDLP EELLRNLYES IKNEPFKIPE DDGNDLTYTF FNPDREGWLL KLGGRVKTWK RRWFILTDNC LYYFEYTTDK EPRGIIPLEN LSIREVEDPR KPNCFELYNP SHKGQVIKAC KTEADGRVVE GNHVVYRISA PSPEEKEEWM KSIKASISRD PFYDMLATRK RRIANKK

Experimental information

• Beam: Instrument name: Advanced Photon Source (APS) BioCAT 18ID / City: Argonne, IL / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.10332 Å / Dist. spec. to detc.: 2 mm
• Detector: Name: MAR 165 CCD

Scan

Title: Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-390)
Measurement date: Mar 21, 2013 / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 1 / Unit: 1/A /

	Min	Max
Q	0.0083	0.3925

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 76 /

	Min	Max
Q	0.00825627	0.392501
P(R) point	1	76
R	0	89

Result

Type of curve: other /

	Experimental	Porod
MW	42.8 kDa	42.8 kDa
Volume	-	64.2 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	1.03	0.002	1.02	0.002
Radius of gyration, Rg	2.86 nm	0.01	2.76 nm	0.02

	Min	Max	Error
D	-	9.3	0.1
Guinier point	1	29	-