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

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Basic information

Entry
Database: SASBDB / ID: SASDCJ6
SampleMmoQ Response regulator (fragment 20-298) from Methylococcus capsulatus str. Bath, Northeast Structural Genomics Consortium Target McR175G
  • MmoQ (protein), Methylococcus capsulatus
Function / homology
Function and homology information


diguanylate cyclase / phosphorelay signal transduction system
Similarity search - Function
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 ...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
Similarity search - Domain/homology
Biological speciesMethylococcus capsulatus (bacteria)
CitationJournal: 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 ...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.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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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)

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Sample

SampleName: MmoQ Response regulator (fragment 20-298) from Methylococcus capsulatus str. Bath, Northeast Structural Genomics Consortium Target McR175G
Specimen concentration: 2.50-5.25
BufferName: 5 mM DTT 100 mM NaCl 10 mM Tris-HCl 0.02 % NaN3 / pH: 7.5
Entity #753Type: 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 ...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

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Experimental information

BeamInstrument name: Stanford Synchrotron Radiation Lightsource (SSRL) BL4-2
City: Stanford, CA / : USA / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.13 Å / Dist. spec. to detc.: 1.5 mm
DetectorName: 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 /
MinMax
Q0.0159 0.3496
Distance distribution function P(R)
Sofotware P(R): GNOM 4.5a / Number of points: 342 /
MinMax
Q0.02338 0.3412
P(R) point8 349
R0 81.95
Result
D max: 8.2 / Type of curve: single_conc /
ExperimentalPorod
MW37.25 kDa37.25 kDa
Volume-61.51 nm3

P(R)Guinier
Forward scattering, I01019 1019.02
Radius of gyration, Rg2.34 nm2.32 nm

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