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- PDB-2mmu: Structure of CrgA, a Cell Division Structural and Regulatory Prot... -

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Basic information

Entry
Database: PDB / ID: 2mmu
TitleStructure of CrgA, a Cell Division Structural and Regulatory Protein from Mycobacterium tuberculosis, in Lipid Bilayers
ComponentsCell division protein CrgA
KeywordsCELL CYCLE / CrgA structure / Membrane protein / Hydrated lipid bilayer
Function / homologyCell division protein CrgA / Cell division protein CrgA / cell cycle / plasma membrane => GO:0005886 / regulation of cell shape / cell division / plasma membrane / Cell division protein CrgA / Cell division protein CrgA
Function and homology information
Biological speciesMycobacterium tuberculosis (bacteria)
MethodSOLID-STATE NMR / simulated annealing, molecular dynamics
Model detailsfewest violations, model1
AuthorsDas, N. / Dai, J. / Hung, I. / Rajagopalan, M. / Zhou, H. / Cross, T.A.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2015
Title: Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.
Authors: Das, N. / Dai, J. / Hung, I. / Rajagopalan, M.R. / Zhou, H.X. / Cross, T.A.
History
DepositionMar 18, 2014Deposition site: BMRB / Processing site: RCSB
Revision 1.0Dec 17, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 31, 2014Group: Database references / Experimental preparation / Structure summary
Revision 1.2Mar 25, 2015Group: Database references
Revision 1.3Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.4May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Cell division protein CrgA


Theoretical massNumber of molelcules
Total (without water)11,5111
Polymers11,5111
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)1 / 1000target function
RepresentativeModel #1fewest violations

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Components

#1: Protein Cell division protein CrgA


Mass: 11510.767 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Strain: H37Rv / Gene: crgA, MT0014, MTCY10H4.11c, Rv0011c / Production host: Escherichia coli (E. coli) / References: UniProt: P67376, UniProt: P9WP57*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLID-STATE NMR
Details: The structure of CrgA, a transmembrane protein of M. tuberculosis in lipid bilayer
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D PISEMA
2222D 13C-13C DARR
2323D NCACX,NCOCX,CAN(CO)CX

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Sample preparation

Details
Solution-IDContentsSolvent system
115NH4Cl - 1.0/13C glucose - 2.0 g/L [U-100% 13C; U-100% 15N] CrgA, 200 mg/mL [U-15N]-Leu CrgA, 200 mg/mL [U-15N]-Ala CrgA, 200 mg/mL [U-15N]-Val CrgA, 200 mg/mL [U-15N]-Ile CrgA, 200 mg/mL [U-15N]-Trp CrgA, 200 mg/mL [U-15N]-Tyr CrgA, 200 mg/mL [U-15N]-Met CrgA, 200 mg/mL [U-15N]-Phe CrgA, 200 mg/mL [U-15N]-Thr CrgA, 200 mg/mL [U-15N]-Gly CrgA, 200 mg/mL [U-15N]-Ser CrgA, 200 mg/mL [U-15N]-Arg CrgA, 200 mg/mL [U-15N]-Asn CrgA, No organic solvent usedNo organic solvent used
215NH4Cl - 1.0/13C glucose - 2.0 g/L [U-100% 13C; U-100% 15N] CrgA uniform label, 13C glucose 2.0 g/L [U-100% 13C] CrgA reverse label (TIFSW not labelled), 13C glucose 2.0 g/L [U-100% 13C] CrgA reverse label (ILFYS not labelled), No organic solvent usedNo organic solvent used
Sample conditions
Conditions-IDpHPressure (kPa)Temperature (K)
18ambient atm289 K
28289 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE6001
Bruker AvanceBrukerAVANCE6002

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Processing

NMR software
NameVersionDeveloperClassification
TopSpin2.1Bruker Biospincollection
TopSpin2.1Bruker Biospinprocessing
Sparky3.114Goddardchemical shift assignment
Sparky3.114Goddarddata analysis
X-PLOR NIH2.34Schwieters, Kuszewski, Tjandra and Clorestructure solution
NAMD2.9(NAMD) Phillips, Braun, Wang, Gumbart, Tajkhorshid, Villa, Chipot, Skeel, Kale and Schultenrefinement
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
RefinementMethod: simulated annealing, molecular dynamics / Software ordinal: 1
NMR constraintsHydrogen bond constraints total count: 56 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 39 / Protein psi angle constraints total count: 39
NMR representativeSelection criteria: fewest violations
NMR ensembleAverage torsion angle constraint violation: 0.69 ° / Conformer selection criteria: target function / Conformers calculated total number: 1000 / Conformers submitted total number: 1 / Maximum torsion angle constraint violation: 3.193 ° / Maximum upper distance constraint violation: 1.489 Å

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