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- SASDFB5: Phosphorylated Resistance to inhibitors of cholinesterase 8 homol... -

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Basic information

Entry
Database: SASBDB / ID: SASDFB5
SamplePhosphorylated Resistance to inhibitors of cholinesterase 8 homolog A, Ric-8A, amino acids 1-452 (Rattus norvegicus)
  • Resistance to inhibitors of cholinesterase 8 homolog A (protein), Ric-8A, Rattus norvegicus
Function / homology
Function and homology information


cell-cell adhesion involved in gastrulation / cell migration involved in gastrulation / basement membrane organization / vasculature development / G-protein alpha-subunit binding / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / guanyl-nucleotide exchange factor activity / visual learning / in utero embryonic development / plasma membrane / cytoplasm
Similarity search - Function
Synembryn / Guanine nucleotide exchange factor, Ric8 / Guanine nucleotide exchange factor synembryn / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
Biological speciesRattus norvegicus (Norway rat)
CitationJournal: Structure / Year: 2019
Title: Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A.
Authors: Baisen Zeng / Tung-Chung Mou / Tzanko I Doukov / Andrea Steiner / Wenxi Yu / Makaia Papasergi-Scott / Gregory G Tall / Franz Hagn / Stephen R Sprang /
Abstract: Ric-8A is a 530-amino acid cytoplasmic molecular chaperone and guanine nucleotide exchange factor (GEF) for i, q, and 12/13 classes of heterortrimeric G protein alpha subunits (Gα). We report the 2. ...Ric-8A is a 530-amino acid cytoplasmic molecular chaperone and guanine nucleotide exchange factor (GEF) for i, q, and 12/13 classes of heterortrimeric G protein alpha subunits (Gα). We report the 2.2-Å crystal structure of the Ric-8A Gα-binding domain with GEF activity, residues 1-452, and is phosphorylated at Ser435 and Thr440. Residues 1-429 adopt a superhelical fold comprised of Armadillo (ARM) and HEAT repeats, and the C terminus is disordered. One of the phosphorylated residues potentially binds to a basic cluster in an ARM motif. Amino acid sequence conservation and published hydrogen-deuterium exchange data indicate repeats 3 through 6 to be a putative Gα-binding surface. Normal mode modeling of small-angle X-ray scattering data indicates that phosphorylation induces relative rotation between repeats 1-4, 5-6, and 7-9. 2D H-N-TROSY spectra of [H,N]-labeled Gαi1 in the presence of R452 reveals chemical shift perturbations of the C terminus and Gαi1 residues involved in nucleotide binding.
Contact author
  • Tung-Chung Mou (university of montana)

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Structure visualization

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Models

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Sample

SampleName: Phosphorylated Resistance to inhibitors of cholinesterase 8 homolog A, Ric-8A, amino acids 1-452 (Rattus norvegicus)
Specimen concentration: 1 mg/ml
BufferName: 25mM HEPES, 150mM NaCl / pH: 8
Entity #1606Name: Ric-8A / Type: protein
Description: Resistance to inhibitors of cholinesterase 8 homolog A
Formula weight: 51.09 / Num. of mol.: 1 / Source: Rattus norvegicus / References: UniProt: B1H241
Sequence: GMEPRAVADA LETGEEDAVT EALRSFNREH SQSFTFDDAQ QEDRKRLAKL LVSVLEQGLS PKHRVTWLQT IRILSRDRSC LDSFASRQSL HALACYADIA ISEEPIPQPP DMDVLLESLK CLCNLVLSSP TAQMLAAEAR LVVRLAERVG LYRKRSYPHE VQFFDLRLLF ...Sequence:
GMEPRAVADA LETGEEDAVT EALRSFNREH SQSFTFDDAQ QEDRKRLAKL LVSVLEQGLS PKHRVTWLQT IRILSRDRSC LDSFASRQSL HALACYADIA ISEEPIPQPP DMDVLLESLK CLCNLVLSSP TAQMLAAEAR LVVRLAERVG LYRKRSYPHE VQFFDLRLLF LLTALRTDVR QQLFQELHGV RLLTDALELT LGVAPKENPL VILPAQETER AMEILKVLFN ITFDSVKREV DEEDAALYRY LGTLLRHCVM ADAAGDRTEE FHGHTVNLLG NLPLKCLDVL LALELHEGSL EFMGVNMDVI NALLAFLEKR LHQTHRLKEC VAPVLSVLTE CARMHRPARK FLKAQVLPPL RDVRTRPEVG DLLRNKLVRL MTHLDTDVKR VAAEFLFVLC SESVPRFIKY TGYGNAAGLL AARGLMAGGR PEGQYSEDED TDTEEYREAK ASI

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Experimental information

BeamInstrument name: Stanford Synchrotron Radiation Lightsource (SSRL) BL4-2
City: Menlo Park, CA / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.1127 Å / Dist. spec. to detc.: 1.7 mm
DetectorName: Rayonix MX225-HE
Scan
Title: Phosphorylated Resistance to inhibitors of cholinesterase 8 homolog A, Ric-8A, amino acids 1-452 (Rattus norvegicus)
Measurement date: Apr 24, 2018 / Storage temperature: 4 °C / Cell temperature: 23 °C / Exposure time: 1 sec. / Number of frames: 25 / Unit: 1/A /
MinMax
Q0.0065 0.4239
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 319 /
MinMax
Q0.0170686 0.185744
P(R) point1 319
R0 101
Result
Type of curve: sec /
ExperimentalPorod
MW51.2 kDa44 kDa
Volume-70 nm3

P(R)GuinierGuinier error
Forward scattering, I084.64 84.58 0.081
Radius of gyration, Rg3.01 nm2.96 nm0.02

MinMax
D-10.1
Guinier point15 69

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