SASDBT9: Full-length human βB2-crystallin (Beta-crystallin B2)

Basic information

• Entry: Database: SASBDB / ID: SASDBT9

Sample

Full-length human βB2-crystallin

• Beta-crystallin B2 (protein), Homo sapiens

Function / homology

Function:

structural constituent of eye lens / lens development in camera-type eye / response to stimulus / visual perception / structural molecule activity / identical protein binding

Domain/homology:

Beta/Gamma crystallin / Crystallins beta and gamma 'Greek key' motif profile. / Beta/gamma crystallins / Beta/gamma crystallin / Gamma-crystallin-like

Component:

Beta-crystallin B2

• Biological species: Homo sapiens (human)
• Citation: Journal: Structure / Year: 2017; Title: Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.; Authors: Zhaoyong Xi / Matthew J Whitley / Angela M Gronenborn / ; Abstract: βγ-Crystallins are long-lived eye lens proteins that are crucial for lens transparency and refractive power. Each βγ-crystallin comprises two homologous domains, which are connected by a short linker. γ-Crystallins are monomeric, while β-crystallins crystallize as dimers and multimers. In the crystal, human βB2-crystallin is a domain-swapped dimer while the N-terminally truncated βB1-crystallin forms a face-en-face dimer. Combining and integrating data from multi-angle light scattering, nuclear magnetic resonance, and small-angle X-ray scattering of full-length and terminally truncated human βB2-crystallin in solution, we show that both these βB2-crystallin proteins are dimeric, possess C2 symmetry, and are more compact than domain-swapped dimers. Importantly, no inter-molecular paramagnetic relaxation enhancement effects compatible with domain swapping were detected. Our collective experimental results unambiguously demonstrate that, in solution, human βB2-crystallin is not domain swapped and exhibits a face-en-face dimer structure similar to the crystal structure of truncated βB1-crystallin.

Contact author

• Zhaoyong Xi (University of Pittsburgh)

Models

• Model #1129: ; Type: dummy / Software: DAMMIN / Radius of dummy atoms: 2.25 A / Chi-square value: 0.144 / P-value: 0.430000; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Full-length human βB2-crystallin / Specimen concentration: 2.2 mg/ml
• Buffer: Name: 25 mM NaPi, 5 mM DTT, 1 mM EDTA, / pH: 6.5

Entity #586

Type: protein / Description: Beta-crystallin B2 / Formula weight: 23.248 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: P43320
Sequence:

ASDHQTQAGK PQSLNPKIII FEQENFQGHS HELNGPCPNL KETGVEKAGS VLVQAGPWVG YEQANCKGEQ FVFEKGEYPR WDSWTSSRRT DSLSSLRPIK VDSQEHKIIL YENPNFTGKK MEIIDDDVPS FHAHGYQEKV SSVRVQSGTW VGYQYPGYRG LQYLLEKGDY KDSSDFGAPH PQVQSVRRIR DMQWHQRGAF HPSN

Experimental information

• Beam: Instrument name: Advanced Photon Source (APS) 12ID-B SAXS/WAXS; City: Argonne, IL / 国: USA / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.08856 Å / Dist. spec. to detc.: 2 mm
• Detector: Name: Pilatus 2M

Scan

Title: full-length βB2-crystallin / Measurement date: Mar 20, 2015 / Exposure time: 0.6 sec. / Number of frames: 30 / Unit: 1/A /

	Min	Max
Q	0.0381	0.4499

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 147 /

	Min	Max
Q	0.038098	0.324963
P(R) point	1	147
R	0	81

Result

Type of curve: single_conc /

	Experimental	Porod
MW	42.1 kDa	42.1 kDa
Volume	-	67.43 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	0.0749	0.0007	0.074	0.001
Radius of gyration, Rg	2.258 nm	0.029	2.238 nm	0.04

	Min	Max
D	-	8.1
Guinier point	1	16