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- PDB-2mzn: NMR structure of the HLTF HIRAN domain in its DNA-bound conformation -

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Basic information

Entry
Database: PDB / ID: 2mzn
TitleNMR structure of the HLTF HIRAN domain in its DNA-bound conformation
ComponentsHelicase-like transcription factor
KeywordsDNA BINDING PROTEIN / HIRAN / HLTF
Function / homology
Function and homology information


hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / ATP-dependent chromatin remodeler activity / regulation of neurogenesis / ATP-dependent activity, acting on DNA / helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / RING-type E3 ubiquitin transferase / mRNA transcription by RNA polymerase II / nuclear matrix / RNA polymerase II transcription regulator complex ...hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / ATP-dependent chromatin remodeler activity / regulation of neurogenesis / ATP-dependent activity, acting on DNA / helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / RING-type E3 ubiquitin transferase / mRNA transcription by RNA polymerase II / nuclear matrix / RNA polymerase II transcription regulator complex / ubiquitin protein ligase activity / E3 ubiquitin ligases ubiquitinate target proteins / protein ubiquitination / DNA repair / ubiquitin protein ligase binding / nucleolus / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / zinc ion binding / nucleoplasm / ATP binding / membrane / nucleus / plasma membrane / cytoplasm
Similarity search - Function
HIRAN domain / HIRAN domain / HIRAN / Zinc finger, C3HC4 type (RING finger) / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. ...HIRAN domain / HIRAN domain / HIRAN / Zinc finger, C3HC4 type (RING finger) / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Helicase conserved C-terminal domain / Zinc finger RING-type profile. / Zinc finger, RING-type / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Zinc finger, RING/FYVE/PHD-type / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Helicase-like transcription factor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsKorzhnev, D. / Eldirany, S.
CitationJournal: Mol.Cell / Year: 2015
Title: HLTF's Ancient HIRAN Domain Binds 3' DNA Ends to Drive Replication Fork Reversal.
Authors: Kile, A.C. / Chavez, D.A. / Bacal, J. / Eldirany, S. / Korzhnev, D.M. / Bezsonova, I. / Eichman, B.F. / Cimprich, K.A.
History
DepositionFeb 18, 2015Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jul 1, 2015Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / 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 / _struct_ref_seq_dif.details
Revision 1.2May 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: Helicase-like transcription factor


Theoretical massNumber of molelcules
Total (without water)13,5321
Polymers13,5321
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)20 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Helicase-like transcription factor / DNA-binding protein/plasminogen activator inhibitor 1 regulator / HIP116 / RING finger protein 80 / ...DNA-binding protein/plasminogen activator inhibitor 1 regulator / HIP116 / RING finger protein 80 / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3 / Sucrose nonfermenting protein 2-like 3


Mass: 13532.326 Da / Num. of mol.: 1 / Fragment: UNP residues 51-171
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLTF, HIP116A, RNF80, SMARCA3, SNF2L3, ZBU1 / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / References: UniProt: Q14527

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1212D 1H-13C HSQC
1313D 1H-13C NOESY
1413D 1H-15N NOESY
1513D (H)CCH-TOCSY
1613D HNCO
1713D HNCA
1813D HN(CO)CA
1912D 1H-13C HSQC aromatic
11013D 1H-13C NOESY CN filtered

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Sample preparation

DetailsContents: 1 mM [U-13C; U-15N] protein, 20 mM sodium phosphate, 100 mM sodium chloride, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1 mMentity-1[U-13C; U-15N]1
20 mMsodium phosphate-21
100 mMsodium chloride-31
Sample conditionsIonic strength: 0.1 / pH: 6.8 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Agilent PremiumCOMPACT / Manufacturer: Agilent / Model: PremiumCOMPACT / Field strength: 800 MHz

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Processing

NMR software
NameDeveloperClassification
SparkyGoddardchemical shift assignment
SparkyGoddarddata analysis
SparkyGoddardpeak picking
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
CNSSOLVEBrunger, Adams, Clore, Gros, Nilges and Readrefinement
CNSSOLVEBrunger, Adams, Clore, Gros, Nilges and Readgeometry optimization
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
ProcheckLaskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thorntondata analysis
TALOSCornilescu, Delaglio and Baxdata analysis
RefinementSoftware ordinal: 1
Details: THE STRUCTURE OF THE 15N/13C-LABELED HIRAN DOMAIN WAS DETERMINED IN THE PRESENCE OF UNLABELED SSDNA (DTTTTTTTTTT). THE DNA STRUCTURE WAS NOT DETERMINED. DNA-BINDING SITE WAS MAPPED USING NMR ...Details: THE STRUCTURE OF THE 15N/13C-LABELED HIRAN DOMAIN WAS DETERMINED IN THE PRESENCE OF UNLABELED SSDNA (DTTTTTTTTTT). THE DNA STRUCTURE WAS NOT DETERMINED. DNA-BINDING SITE WAS MAPPED USING NMR CHEMICAL SHIFT CHANGES. THE VALUES OF DNA-BINDING INDUCED CHEMICAL SHIFT CHANGES ARE AVAILABLE AS PART OF BMRB DEPOSITION 25492.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 20

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