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- PDB-2g0u: Solution Structure of Monomeric BsaL, the Type III Secretion Need... -

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Basic information

Entry
Database: PDB / ID: 2g0u
TitleSolution Structure of Monomeric BsaL, the Type III Secretion Needle Protein of Burkholderia pseudomallei
Componentstype III secretion system needle protein
KeywordsUNKNOWN FUNCTION / helix-turn-helix
Function / homology
Function and homology information


type III protein secretion system complex / protein secretion by the type III secretion system / cell surface / extracellular region
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #90 / Type III secretion, needle-protein-like / Type III secretion, needle-protein-like superfamily / Type III secretion needle MxiH, YscF, SsaG, EprI, PscF, EscF / Type III secretion system, needle protein / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Type III secretion system protein
Similarity search - Component
Biological speciesBurkholderia pseudomallei (bacteria)
MethodSOLUTION NMR / torsion angle dynamics simulated annealing, molecular dynamics
AuthorsZhang, L. / Wang, Y. / Picking, W.L. / Picking, W.D. / De Guzman, R.N.
CitationJournal: J.Mol.Biol. / Year: 2006
Title: Solution Structure of Monomeric BsaL, the Type III Secretion Needle Protein of Burkholderia pseudomallei.
Authors: Zhang, L. / Wang, Y. / Picking, W.L. / Picking, W.D. / De Guzman, R.N.
History
DepositionFeb 13, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 23, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: type III secretion system needle protein


Theoretical massNumber of molelcules
Total (without water)10,3681
Polymers10,3681
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 200structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein type III secretion system needle protein


Mass: 10368.455 Da / Num. of mol.: 1 / Fragment: BsaLdelta5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Burkholderia pseudomallei (bacteria) / Strain: E264 / Production host: Escherichia coli (E. coli) / References: UniProt: Q63K18

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1213D 13C-separated NOESY
131

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Sample preparation

Sample conditionsIonic strength: 20mM / pH: 7 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE8001
Varian INOVAVarianINOVA6002

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Processing

NMR software
NameVersionDeveloperClassification
NMRPipe2005Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A.processing
NMRView5.0.2Johnson, B.A.data analysis
CYANAGuntert, P.refinement
Amber7Case, D.A., Pearlman, D.A., Caldwell, J.W., Cheatham III, T.E., Wang, J., Ross, W.S., Simmerling, C.L., Darden, T.A., Merz, K.M., Stanton, R.V., Cheng, A.L., Vincent, J.J., Crowley, M., Tsui, V., Gohlke, H., Radmer, R.J., Duan, Y., Pitera, J., Massova, I., Seibel, G.L., Singh, U.C., Weiner, P.K., and Kollman, P.A.refinement
RefinementMethod: torsion angle dynamics simulated annealing, molecular dynamics
Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 20

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