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- PDB-1k1c: Solution Structure of Crh, the Bacillus subtilis Catabolite Repre... -

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Basic information

Entry
Database: PDB / ID: 1k1c
TitleSolution Structure of Crh, the Bacillus subtilis Catabolite Repression HPr
Componentscatabolite repression HPr-like protein
KeywordsTRANSPORT PROTEIN / open-faced b-sandwich / phosphotransferase system / carbon catabolite repression
Function / homology
Function and homology information


Phosphotransferase system, HPr serine phosphorylation site / PTS HPR domain serine phosphorylation site signature. / HPr-like / Histidine-containing Protein; Chain: A; / Phosphocarrier protein HPr-like / HPr-like superfamily / PTS HPr component phosphorylation site / PTS HPR domain profile. / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
HPr-like protein Crh
Similarity search - Component
Biological speciesBacillus subtilis (bacteria)
MethodSOLUTION NMR / simulated annealing, molecular dynamics
AuthorsFavier, A. / Brutscher, B. / Blackledge, M. / Galinier, A. / Deutscher, J. / Penin, F. / Marion, D.
Citation
Journal: J.Mol.Biol. / Year: 2002
Title: Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr.
Authors: Favier, A. / Brutscher, B. / Blackledge, M. / Galinier, A. / Deutscher, J. / Penin, F. / Marion, D.
#1: Journal: J.Mol.Microbiol.Biotechnol. / Year: 2001
Title: Evidence for a Dimerisation State of the Bacillus subtilis Catabolite Repression HPr-like Protein, Crh
Authors: Penin, F. / Favier, A. / Montserret, R. / Brutscher, B. / Deutscher, J. / Marion, D. / Galinier, D.
History
DepositionSep 25, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 17, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: catabolite repression HPr-like protein


Theoretical massNumber of molelcules
Total (without water)9,2051
Polymers9,2051
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)24 / 250structures with the least restraint violations
RepresentativeModel #16closest to the average

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Components

#1: Protein catabolite repression HPr-like protein


Mass: 9205.473 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus subtilis (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: O06976

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1223D 13C-separated NOESY
132HNCA-J
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy.

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Sample preparation

Details
Solution-IDContentsSolvent system
10.5mM Crh, 15N, 20 mM sodium phosphate buffer, 50 mM NaCl, 0.05% sodium azide90% H2O/10% D2O
20.5mM Crh, 15N 13C, 20 mM sodium phosphate buffer, 50 mM NaCl, 0.05% sodium azide90% H2O/10% D2O
Sample conditionsIonic strength: 50 mM NaCl / pH: 7.5 / Pressure: ambient / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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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
Varian INOVAVarianINOVA6001
Varian INOVAVarianINOVA8002

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Processing

NMR software
NameVersionDeveloperClassification
Discover95MSIstructure solution
Amber4Cornell et al.refinement
Felix2000MSIprocessing
VNMR6.AVARIANcollection
Insight II97MSIdata analysis
RefinementMethod: simulated annealing, molecular dynamics / Software ordinal: 1
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 250 / Conformers submitted total number: 24

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