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- SASDAQ8: kLANA mutant dimer-tetramer mixture (ORF73 tetramer, kLANA mutant... -

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Basic information

Entry
Database: SASBDB / ID: SASDAQ8
SamplekLANA mutant dimer-tetramer mixture
  • ORF73 tetramer (protein), kLANA mutant K1109E, Human herpesvirus 8
  • ORF73 dimer (protein), kLANA mutant K1109E, Human herpesvirus 8
Function / homology: / Protein LANA1-like, DNA-binding domain / Epstein Barr virus nuclear antigen-1, DNA-binding domain superfamily / viral life cycle / : / host cell nucleus / DNA binding / Protein LANA1
Function and homology information
Biological speciesHuman herpesvirus 8
CitationJournal: Nucleic Acids Res / Year: 2015
Title: KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA.
Authors: Rajesh Ponnusamy / Maxim V Petoukhov / Bruno Correia / Tania F Custodio / Franceline Juillard / Min Tan / Marta Pires de Miranda / Maria A Carrondo / J Pedro Simas / Kenneth M Kaye / Dmitri ...Authors: Rajesh Ponnusamy / Maxim V Petoukhov / Bruno Correia / Tania F Custodio / Franceline Juillard / Min Tan / Marta Pires de Miranda / Maria A Carrondo / J Pedro Simas / Kenneth M Kaye / Dmitri I Svergun / Colin E McVey /
Abstract: Latency-associated nuclear antigen (LANA) is central to episomal tethering, replication and transcriptional regulation of γ2-herpesviruses. LANA binds cooperatively to the terminal repeat (TR) ...Latency-associated nuclear antigen (LANA) is central to episomal tethering, replication and transcriptional regulation of γ2-herpesviruses. LANA binds cooperatively to the terminal repeat (TR) region of the viral episome via adjacent LANA binding sites (LBS), but the molecular mechanism by which LANA assembles on the TR remains elusive. We show that KSHV LANA and MHV-68 LANA proteins bind LBS DNA using strikingly different modes. Solution structure of LANA complexes revealed that while kLANA tetramer is intrinsically bent both in the free and bound state to LBS1-2 DNA, mLANA oligomers instead adopt a rigid linear conformation. In addition, we report a novel non-ring kLANA structure that displays more flexibility at its assembly interface than previously demonstrated. We identified a hydrophobic pivot point located at the dimer-dimer assembly interface, which gives rotational freedom for kLANA to adopt variable conformations to accommodate both LBS1-2 and LBS2-1-3 DNA. Alterations in the arrangement of LBS within TR or at the tetramer assembly interface have a drastic effect on the ability of kLANA binding. We also show kLANA and mLANA DNA binding functions can be reciprocated. Although KSHV and MHV-68 are closely related, the findings provide new insights into how the structure, oligomerization, and DNA binding of LANA have evolved differently to assemble on the TR DNA.
Contact author
  • Maxim Petoukhov (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #335
Type: mix / Software: oligomer / Radius of dummy atoms: 1.90 A / Chi-square value: 0.83
Search similar-shape structures of this assembly by Omokage search (details)
Model #336
Type: mix / Software: oligomer / Radius of dummy atoms: 1.90 A / Chi-square value: 0.83
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: kLANA mutant dimer-tetramer mixture / Specimen concentration: 2.5 mg/ml / Entity id: 196 / 197
BufferName: 25 mM Na/K Phosphate / pH: 7.5
Entity #196Name: kLANA mutant K1109E / Type: protein / Description: ORF73 tetramer / Formula weight: 15.759 / Num. of mol.: 4 / Source: Human herpesvirus 8 / References: UniProt: Q9QR71
Sequence:
SHPRYQQPPV PYRQIDDCPA KARPQHIFYR RFLGKDGRRD PKCQWKFAVI FWGNDPYGLK KLSQAFQFGG VKAGPVSCLP HPGPDQSPIT YCVYVYCQNK DTSKKVQMAR LAWEASHPLA GNLQSSIVKF KKPLPLTQ
Entity #197Name: kLANA mutant K1109E / Type: protein / Description: ORF73 dimer / Formula weight: 15.759 / Num. of mol.: 2 / Source: Human herpesvirus 8 / References: UniProt: Q9QR71
Sequence:
SHPRYQQPPV PYRQIDDCPA KARPQHIFYR RFLGKDGRRD PKCQWKFAVI FWGNDPYGLK KLSQAFQFGG VKAGPVSCLP HPGPDQSPIT YCVYVYCQNK DTSKKVQMAR LAWEASHPLA GNLQSSIVKF KKPLPLTQ

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Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.93 Å / Dist. spec. to detc.: 2.43 mm
DetectorName: Pilatus 1M
Scan
Title: kLANA mutant mixture / Measurement date: Jun 21, 2014 / Unit: 1/nm /
MinMax
Q0.1552 4.9674
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 491 /
MinMax
Q0.155196 2.47606
P(R) point1 491
R0 9.5
Result
D max: 9.5 / Type of curve: single_conc
Comments: Study of oligomeric states of mLANA and kLANA and their complexes with DNA
ExperimentalStandardPorod
MW30 kDa30 kDa30 kDa
Volume--50 nm3

GuinierP(R)
Forward scattering, I035 -
Radius of gyration, Rg2.4 nm2.4 nm

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