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- PDB-1r05: Solution Structure of Max B-HLH-LZ -

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Basic information

Entry
Database: PDB / ID: 1r05
TitleSolution Structure of Max B-HLH-LZ
ComponentsMax protein
KeywordsTRANSCRIPTION / Basic-Helix-Loop-Helix-LeucineZipper Homodimer
Function / homology
Function and homology information


Mad-Max complex / Myc-Max complex / Transcription of E2F targets under negative control by DREAM complex / E-box binding / Transcriptional Regulation by E2F6 / MLL1 complex / Cyclin E associated events during G1/S transition / Cyclin A:Cdk2-associated events at S phase entry / protein-DNA complex / DNA-binding transcription repressor activity, RNA polymerase II-specific ...Mad-Max complex / Myc-Max complex / Transcription of E2F targets under negative control by DREAM complex / E-box binding / Transcriptional Regulation by E2F6 / MLL1 complex / Cyclin E associated events during G1/S transition / Cyclin A:Cdk2-associated events at S phase entry / protein-DNA complex / DNA-binding transcription repressor activity, RNA polymerase II-specific / RNA polymerase II transcription regulator complex / sequence-specific double-stranded DNA binding / DNA-binding transcription factor binding / protein dimerization activity / DNA-binding transcription factor activity, RNA polymerase II-specific / DNA-binding transcription factor activity / dendrite / chromatin / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / identical protein binding / nucleus
Similarity search - Function
Helix-loop-helix DNA-binding domain / MYOD Basic-Helix-Loop-Helix Domain, subunit B / Helix-loop-helix DNA-binding domain / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain / Myc-type, basic helix-loop-helix (bHLH) domain profile. / Helix-loop-helix DNA-binding domain superfamily / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsSauv, S. / Tremblay, L. / Lavigne, P.
CitationJournal: J.Mol.Biol. / Year: 2004
Title: The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors
Authors: Sauv, S. / Tremblay, L. / Lavigne, P.
History
DepositionSep 19, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 21, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 27, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Max protein
B: Max protein


Theoretical massNumber of molelcules
Total (without water)20,3472
Polymers20,3472
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)6 / -
Representative

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Components

#1: Protein Max protein / Max B-HLH-LZ


Mass: 10173.514 Da / Num. of mol.: 2 / Mutation: N58V, H61L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MAX / Production host: Escherichia coli (E. coli) / References: UniProt: P61244

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N-NOESYHSQC
12213C-NOESYHSQC
13213C-(H)CCH-TOCSY
14213C-(H)CCH-COSY
152Triple Resonance, such as HNCA and HN(CA)CB

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Sample preparation

Details
Solution-IDContentsSolvent system
125mM Max 15N, 50mM Phosphate buffer, 250mM KCl90% H2O/10% D2O
225mM Max 13C,15N, 50mM Phosphate buffer, 250mM KCl90% H2O/10% D2O
Sample conditionsIonic strength: 250mM KCl / pH: 6.8 / Pressure: ambient / Temperature: 308 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 spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
NMRPipeFrank Delaglio, et al.structural assignment
X-PLORBrunger, et al.refinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformers submitted total number: 6

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