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- PDB-2xxs: Solution structure of the N-terminal domain of the Shigella type ... -

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Basic information

Entry
Database: PDB / ID: 2xxs
TitleSolution structure of the N-terminal domain of the Shigella type III secretion protein MxiG
ComponentsPROTEIN MXIG
KeywordsPROTEIN BINDING / PATHOGENESIS / TRANSPORT / VIRULENCE / BASAL BODY STRUCTURAL COMPONENT
Function / homologyTumour Suppressor Smad4 - #50 / Type III secretion system, PrgH/EprH-like / Type III secretion system protein PrgH-EprH (PrgH) / Tumour Suppressor Smad4 / cell outer membrane / Sandwich / Mainly Beta / plasma membrane / Protein MxiG
Function and homology information
Biological speciesSHIGELLA FLEXNERI (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsMcDowell, M.A. / Johnson, S. / Deane, J.E. / McDonnell, J.M. / Lea, S.M.
CitationJournal: J.Biol.Chem. / Year: 2011
Title: Structural and Functional Studies on the N-Terminal Domain of the Shigella Type III Secretion Protein Mxig.
Authors: Mcdowell, M.A. / Johnson, S. / Deane, J.E. / Cheung, M. / Roehrich, A.D. / Blocker, A.J. / Mcdonnell, J.M. / Lea, S.M.
History
DepositionNov 11, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 6, 2011Provider: repository / Type: Initial release
Revision 1.1Sep 7, 2011Group: Database references / Version format compliance
Revision 2.0May 15, 2024Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Other
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN MXIG


Theoretical massNumber of molelcules
Total (without water)12,1801
Polymers12,1801
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 / 350LOWEST TARGET FUNCTION
RepresentativeModel #1

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Components

#1: Protein PROTEIN MXIG / MXIG


Mass: 12180.494 Da / Num. of mol.: 1
Fragment: N-TERMINAL FORKHEAD ASSOCIATED DOMAIN, RESIDUES 6-112
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SHIGELLA FLEXNERI (bacteria) / Strain: 301 / Variant: SEROTYPE 2A / Plasmid: PET14B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0A221

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HN(CO)CA
121CBCA(CO)NH
131CBCANH
141HNCO
151CC(CO)NH
161H(CCCO)NH
17115N-NOESY-HSQC
18113C-NOESY
191CLEANEX-PM
1101LONG-RANGE HNCO
1111HNHA
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C AND 15N LABELED MXIG N-TERMINAL DOMAIN. NOESY EXPERIMENTS PROVIDED THE INPUT DISTANCE RESTRAINTS, WHILST A LONG-RANGE ...Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C AND 15N LABELED MXIG N-TERMINAL DOMAIN. NOESY EXPERIMENTS PROVIDED THE INPUT DISTANCE RESTRAINTS, WHILST A LONG-RANGE HNCO EXPERIMENT INDICATED HYDROGEN BONDS. DIHEDRAL ANGLE RESTRAINTS WERE CALCULATED FROM A HNHA EXPERIMENT AND PREDICTED BY TALOSPLUS

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Sample preparation

DetailsContents: 25MM NAPI, 1MM DTT, 5% D2O
Sample conditionspH: 6.8 / Temperature: 298.0 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz

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Processing

NMR software
NameDeveloperClassification
DYANAP.GUENTERT,C.MUMENTHALER,K.WUETHRICHrefinement
DYANAstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: LOWEST TARGET FUNCTION / Conformers calculated total number: 350 / Conformers submitted total number: 20

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