SASDCJ6: MmoQ Response regulator (fragment 20-298) from Methylococcus caps...

Basic information

• Entry: Database: SASBDB / ID: SASDCJ6

Sample

MmoQ Response regulator (fragment 20-298) from Methylococcus capsulatus str. Bath, Northeast Structural Genomics Consortium Target McR175G

• MmoQ (protein), Methylococcus capsulatus

Function / homology

Function:

negative regulation of bacterial-type flagellum-dependent cell motility / diguanylate cyclase / diguanylate cyclase activity / cell adhesion involved in single-species biofilm formation / phosphorelay signal transduction system / plasma membrane

Domain/homology:

Metal-dependent hydrolase HDOD / HDOD domain / HD-related output (HDOD) domain profile. / : / Diguanylate cyclase, GGDEF domain / diguanylate cyclase / GGDEF domain profile. / GGDEF domain / Nucleotide cyclase / Response regulator receiver domain / cheY-homologous receiver domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily / Reverse transcriptase/Diguanylate cyclase domain

Component:

diguanylate cyclase

• Biological species: Methylococcus capsulatus (bacteria)
• Citation: Journal: Biopolymers / Year: 2011; Title: Small angle X-ray scattering as a complementary tool for high-throughput structural studies.; Authors: Thomas D Grant / Joseph R Luft / Jennifer R Wolfley / Hiro Tsuruta / Anne Martel / Gaetano T Montelione / Edward H Snell / ; Abstract: Structural crystallography and nuclear magnetic resonance (NMR) spectroscopy are the predominant techniques for understanding the biological world on a molecular level. Crystallography is constrained by the ability to form a crystal that diffracts well and NMR is constrained to smaller proteins. Although powerful techniques, they leave many soluble, purified structurally uncharacterized protein samples. Small angle X-ray scattering (SAXS) is a solution technique that provides data on the size and multiple conformations of a sample, and can be used to reconstruct a low-resolution molecular envelope of a macromolecule. In this study, SAXS has been used in a high-throughput manner on a subset of 28 proteins, where structural information is available from crystallographic and/or NMR techniques. These crystallographic and NMR structures were used to validate the accuracy of molecular envelopes reconstructed from SAXS data on a statistical level, to compare and highlight complementary structural information that SAXS provides, and to leverage biological information derived by crystallographers and spectroscopists from their structures. All the ab initio molecular envelopes calculated from the SAXS data agree well with the available structural information. SAXS is a powerful albeit low-resolution technique that can provide additional structural information in a high-throughput and complementary manner to improve the functional interpretation of high-resolution structures.

Models

• Model #1437: ; Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 8.497225; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1438: ; Type: dummy / Radius of dummy atoms: 2.00 A / Chi-square value: 2.319529; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: MmoQ Response regulator (fragment 20-298) from Methylococcus capsulatus str. Bath, Northeast Structural Genomics Consortium Target McR175G; Specimen concentration: 2.50-5.25
• Buffer: Name: 5 mM DTT 100 mM NaCl 10 mM Tris-HCl 0.02 % NaN3 / pH: 7.5

Entity #753

Type: protein / Description: MmoQ / Formula weight: 32.023 / Num. of mol.: 1 / Source: Methylococcus capsulatus / References: UniProt: Q7WZ31
Sequence:

MDRWNMHKPM LCDSLPTASR TAAAILNLAQ REDVTAEALA QLIQTDPALT GRILRFANAP AQGTRRPVAS VIDAIDLVGL PAVRQFALSL SLIDAHREGR CEAFDYAAYW QKSLARAVAL QSITAQASTV APKEAFTLGL LADVGRLALA TAWPEEYSEC LRKADGEALI ALERERFATD HDELTRMLLT DWGFPQVFID ALQLSQQDEI RDEGRTGRFA RQLALAQHIA DHRLAEEPRR AALSPLLRAE ARRCGLGDED LARLLADPPA DWLDWTRTIG LEHHHHHH

Experimental information

• Beam: Instrument name: Stanford Synchrotron Radiation Lightsource (SSRL) BL4-2; City: Stanford, CA / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.13 Å / Dist. spec. to detc.: 1.5 mm
• Detector: Name: Rayonix MX225-HE

Scan

Title: MmoQ Response regulator (fragment 20-298) from Methylococcus capsulatus str. Bath, Northeast Structural Genomics Consortium Target McR175G
Measurement date: Feb 12, 2010 / Storage temperature: -80 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 20 / Unit: 1/A /

	Min	Max
Q	0.0159	0.3496

Distance distribution function P(R)

Sofotware P(R): GNOM 4.5a / Number of points: 342 /

	Min	Max
Q	0.02338	0.3412
P(R) point	8	349
R	0	81.95

Result

D max: 8.2 / Type of curve: single_conc /

	Experimental	Porod
MW	37.25 kDa	37.25 kDa
Volume	-	61.51 nm3

	P(R)	Guinier
Forward scattering, I0	1019	1019.02
Radius of gyration, Rg	2.34 nm	2.32 nm