Crystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA.

2.50
Hdl Handle:
http://hdl.handle.net/10033/561317
Title:
Crystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA.
Authors:
Hellert, Jan; Krausze, Joern; Schulz, Thomas F; Lührs, Thorsten
Abstract:
The latency-associated nuclear antigen (LANA) is the latent origin-binding protein and chromatin anchor of the Kaposi's sarcoma herpesvirus (KSHV/HHV-8) genome. Its C-terminal domain (CTD) binds sequence-specifically to the viral origin of replication, whereas the N-terminal domain links it to nucleosomes of cellular chromatin for long-term persistence in dividing host cells. Here, the crystallization and X-ray data acquisition of a mutant LANA CTD in complex with its wild-type target DNA LBS1 is described. This report describes the rational protein engineering for successful co-crystallization with DNA and X-ray diffraction data collection at room temperature on the high-brilliance third-generation synchrotron PETRA III at DESY, Germany.
Affiliation:
Helmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.
Citation:
Crystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA. 2014, 70 (Pt 11):1570-4 Acta Crystallogr F Struct Biol Commun
Journal:
Acta crystallographica. Section F, Structural biology communications
Issue Date:
Nov-2014
URI:
http://hdl.handle.net/10033/561317
DOI:
10.1107/S2053230X14019906
PubMed ID:
25372834
Type:
Article
Language:
en
ISSN:
2053-230X
Appears in Collections:
Publications of the Dept. Structure and Functions of Proteins(SFPR)

Full metadata record

DC FieldValue Language
dc.contributor.authorHellert, Janen
dc.contributor.authorKrausze, Joernen
dc.contributor.authorSchulz, Thomas Fen
dc.contributor.authorLührs, Thorstenen
dc.date.accessioned2015-07-31T14:30:59Zen
dc.date.available2015-07-31T14:30:59Zen
dc.date.issued2014-11en
dc.identifier.citationCrystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA. 2014, 70 (Pt 11):1570-4 Acta Crystallogr F Struct Biol Communen
dc.identifier.issn2053-230Xen
dc.identifier.pmid25372834en
dc.identifier.doi10.1107/S2053230X14019906en
dc.identifier.urihttp://hdl.handle.net/10033/561317en
dc.description.abstractThe latency-associated nuclear antigen (LANA) is the latent origin-binding protein and chromatin anchor of the Kaposi's sarcoma herpesvirus (KSHV/HHV-8) genome. Its C-terminal domain (CTD) binds sequence-specifically to the viral origin of replication, whereas the N-terminal domain links it to nucleosomes of cellular chromatin for long-term persistence in dividing host cells. Here, the crystallization and X-ray data acquisition of a mutant LANA CTD in complex with its wild-type target DNA LBS1 is described. This report describes the rational protein engineering for successful co-crystallization with DNA and X-ray diffraction data collection at room temperature on the high-brilliance third-generation synchrotron PETRA III at DESY, Germany.en
dc.language.isoenen
dc.subject.meshAntigens, Viralen
dc.subject.meshCrystallizationen
dc.subject.meshDNA, Viralen
dc.subject.meshHerpesvirus 8, Humanen
dc.subject.meshNuclear Proteinsen
dc.subject.meshProtein Structure, Secondaryen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshSarcoma, Kaposien
dc.subject.meshX-Ray Diffractionen
dc.titleCrystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.en
dc.identifier.journalActa crystallographica. Section F, Structural biology communicationsen
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