+Open data
-Basic information
Entry | Database: PDB / ID: 2oar | |||||||||
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Title | Mechanosensitive Channel of Large Conductance (MscL) | |||||||||
Components | Large-conductance mechanosensitive channel | |||||||||
Keywords | MEMBRANE PROTEIN / stretch activated ion channel mechanosensitive | |||||||||
Function / homology | Function and homology information gated channel activity / intracellular water homeostasis / plasma membrane => GO:0005886 / mechanosensitive monoatomic ion channel activity / monoatomic ion transport / membrane => GO:0016020 / transmembrane transport / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Mycobacterium tuberculosis H37Ra (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 3.5 Å | |||||||||
Authors | Rees, D.C. / Chang, G. / Spencer, R.H. / Lee, A.T. / Steinbacher, S. / Strop, P. | |||||||||
Citation | Journal: Current Topics in Membranes / Year: 2007 Title: Structures of the Prokaryotic Mechanosensitive Channels MscL and MscS Authors: Steinbacher, S. / Bass, R. / Strop, P. / Rees, D.C. #1: Journal: Science / Year: 1998 Title: Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel Authors: Chang, G. / Spencer, R.H. / Lee, A.T. / Barclay, M.T. / Rees, D.C. #2: Journal: METHODS AND RESULTS IN CRYSTALLIZATION OF MEMBRANE PROTEINS Year: 2003 Title: Crystallization and structure determination of MSCL, a gated prokaryotic mechanosensitive channel | |||||||||
History |
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Remark 999 | SEQUENCE All the non-histidine residues in the N-terminal 22 residues are part of a cleavable his- ...SEQUENCE All the non-histidine residues in the N-terminal 22 residues are part of a cleavable his-tag construct that was added to the MscL sequence. The protein sequence is not cleaved |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2oar.cif.gz | 131.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2oar.ent.gz | 103.8 KB | Display | PDB format |
PDBx/mmJSON format | 2oar.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2oar_validation.pdf.gz | 481 KB | Display | wwPDB validaton report |
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Full document | 2oar_full_validation.pdf.gz | 528.5 KB | Display | |
Data in XML | 2oar_validation.xml.gz | 29.7 KB | Display | |
Data in CIF | 2oar_validation.cif.gz | 39 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oa/2oar ftp://data.pdbj.org/pub/pdb/validation_reports/oa/2oar | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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Details | The asymmetric unit contains one pentamer which is the biological unit |
-Components
#1: Protein | Mass: 18817.307 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium tuberculosis H37Ra (bacteria) Species: Mycobacterium tuberculosis / Strain: H37RA / Gene: mscL / Plasmid: pET19B / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P0A5K8, UniProt: A5U127*PLUS #2: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 5.9 Å3/Da / Density % sol: 78.97 % |
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Crystal grow | Method: vapor diffusion, sitting drop / pH: 3.7 Details: PROTEIN CONCENTRATION 15-20 MG/ML AND 0.05% DODECYLMALTOSIDE.PROTEIN WAS MIXED IN A RATIO OF 4:3 OR 3:2 WITH THE RESERVOIR SOLUTION CONTAINING 100-120 mM AMMONIUM SULFUATE, 23-27% ...Details: PROTEIN CONCENTRATION 15-20 MG/ML AND 0.05% DODECYLMALTOSIDE.PROTEIN WAS MIXED IN A RATIO OF 4:3 OR 3:2 WITH THE RESERVOIR SOLUTION CONTAINING 100-120 mM AMMONIUM SULFUATE, 23-27% TRIETHYLENE GLYCOL, 100 mM GLYCINE, WITH 1-3 mM GD(CL)3 OR SM(CL)3 AND D2O AS THE SOLVENT. 1 mM (NA3)AU(S2O3)2 WAS SOAKED INTO THE CRYSTAL, pH 3.7, VAPOR DIFFUSION, SITTING DROP |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.98 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 3.5→20 Å / Num. obs: 25597 / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Rsym value: 0.103 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 3.5→3.6 Å / Redundancy: 1.3 % / Mean I/σ(I) obs: 1 / Rsym value: 0.458 / % possible all: 50.4 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 3.5→20 Å / σ(F): 1
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Solvent computation | Bsol: 40 Å2 / ksol: 0.25 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 135.31 Å2
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Refinement step | Cycle: LAST / Resolution: 3.5→20 Å
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Refine LS restraints |
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Xplor file |
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