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- SASDCE6: PAS domain of the protein CPS_1291 from Colwellia psychrerythraea... -

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ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDCE6
SamplePAS domain of the protein CPS_1291 from Colwellia psychrerythraea. Northeast Structural Genomics Consortium target id CsR222B
  • Sensory box/GGDEF domain protein (protein), Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Function / homology
Function and homology information


: / PAS fold-3 / PAS fold / Diguanylate cyclase, GGDEF domain / diguanylate cyclase / GGDEF domain profile. / GGDEF domain / PAS-associated, C-terminal / PAC domain profile. / Nucleotide cyclase ...: / PAS fold-3 / PAS fold / Diguanylate cyclase, GGDEF domain / diguanylate cyclase / GGDEF domain profile. / GGDEF domain / PAS-associated, C-terminal / PAC domain profile. / Nucleotide cyclase / PAC motif / Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) / PAS domain / PAS repeat profile. / PAS domain / PAS domain superfamily / Reverse transcriptase/Diguanylate cyclase domain
Similarity search - Domain/homology
Sensory box/GGDEF domain protein
Similarity search - Component
Biological speciesColwellia psychrerythraea (strain 34H / ATCC BAA-681) (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 #1423
Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 14.402025
Search similar-shape structures of this assembly by Omokage search (details)
Model #1424
Type: dummy / Radius of dummy atoms: 2.00 A / Chi-square value: 2.477476
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: PAS domain of the protein CPS_1291 from Colwellia psychrerythraea. Northeast Structural Genomics Consortium target id CsR222B
Specimen concentration: 1.89-6.93
BufferName: 5 mM DTT 100 mM NaCl 10 mM Tris-HCl 0.02 % NaN3 / pH: 7.5
Entity #749Type: protein / Description: Sensory box/GGDEF domain protein / Formula weight: 15.107 / Num. of mol.: 2
Source: Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
References: UniProt: Q486I1
Sequence:
MNVDILKQRA KAFDYVFDAI VVTDLQGFII DWNKGSETLY GYSKEQAIGQ PVNMLHVPGD TEHITSEVIS AVENQGKWTG EIRMLHKDGH IGWIESMCVP IYGENYQMVG ALGINRDITK RKKELEHHHH HH

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Experimental information

BeamInstrument name: Stanford Synchrotron Radiation Lightsource (SSRL) BL4-2
City: Stanford, CA / : USA / Type of source: X-ray synchrotron / Wavelength: 0.13 Å / Dist. spec. to detc.: 1.5 mm
DetectorName: Rayonix MX225-HE
Scan
Title: PAS domain of the protein CPS_1291 from Colwellia psychrerythraea. Northeast Structural Genomics Consortium target id CsR222B
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: 358 /
MinMax
Q0.01685 0.3496
P(R) point1 358
R0 76.81
Result
D max: 7.68 / Type of curve: single_conc /
ExperimentalPorod
MW31.41 kDa31.41 kDa
Volume-52.14 nm3

P(R)Guinier
Forward scattering, I02157 2157.41
Radius of gyration, Rg2.25 nm2.24 nm

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