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- SASDAM8: MHV-68 LANA (Latency-associated nuclear antigen, mLANA) -

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Basic information

Entry
Database: SASBDB / ID: SASDAM8
SampleMHV-68 LANA
  • Latency-associated nuclear antigen (protein), mLANA, Murid herpesvirus 4
Function / homology: / Protein LANA1-like, DNA-binding domain / Epstein Barr virus nuclear antigen-1, DNA-binding domain superfamily / host cell nucleus / DNA binding / identical protein binding / 73 protein
Function and homology information
Biological speciesMurid herpesvirus 4 (Murine herpesvirus 68)
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 #326
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.69
Search similar-shape structures of this assembly by Omokage search (details)
Model #327
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.69
Search similar-shape structures of this assembly by Omokage search (details)
Model #328
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.69
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: MHV-68 LANA / Specimen concentration: 5 mg/ml
BufferName: 25 mM Na/K Phosphate / pH: 7.5
Entity #193Name: mLANA / Type: protein / Description: Latency-associated nuclear antigen / Formula weight: 21.721 / Num. of mol.: 4 / Source: Murid herpesvirus 4 / References: UniProt: O41974
Sequence: MPTSPPTTRN TTSGKTRSGC KRRCFNKPAA MPPKRRRAPK RPAPPPPPGC QGDEESSQGT QTPNPPSPPV PPSSPTLPSS PVPPSSPVHE PPSPSPPPAP PSPDVDVEGL DVGETDDPGP PPPKRYSRYQ KPHNPSDPLP KKYQGMRRHL QVTAPRLFDP EGHPPTHFKS ...Sequence:
MPTSPPTTRN TTSGKTRSGC KRRCFNKPAA MPPKRRRAPK RPAPPPPPGC QGDEESSQGT QTPNPPSPPV PPSSPTLPSS PVPPSSPVHE PPSPSPPPAP PSPDVDVEGL DVGETDDPGP PPPKRYSRYQ KPHNPSDPLP KKYQGMRRHL QVTAPRLFDP EGHPPTHFKS AVMFSSTHPY TLNKLHKCIQ SKHVLSTPVS CLPLVPGTTQ QCVTYYLLSF VEDKKQAKKL KRVVLAYCEK YHSSVEGTIV KAKPYFPLPE PPTEPPTDPE QPSTSTQASG TQHGPTASLD AGAEQGATGS PGSSPGQQGQ GSQT

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Experimental information

BeamInstrument name: PETRA III P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 2M
Scan
Title: mLANA / Measurement date: Apr 27, 2013 / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.1882 4.6092
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 731 /
MinMax
Q0.188184 2.10351
P(R) point1 731
R0 16.12
Result
D max: 16 / Type of curve: single_conc
Comments: Study of oligomeric states of mLANA and kLANA and their complexes with DNA
ExperimentalPorod
MW100 kDa100 kDa
Volume-117 nm3

GuinierP(R)
Forward scattering, I04845 -
Radius of gyration, Rg4.2 nm4.4 nm

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