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Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H.


ABSTRACT: RNase H (retroviral ribonuclease H) cleaves the phosphate backbone of the RNA template within an RNA/DNA hybrid to complete the synthesis of double-stranded viral DNA. In the present study we have determined the complete structure of the RNase H domain from XMRV (xenotropic murine leukaemia virus-related virus) RT (reverse transcriptase). The basic protrusion motif of the XMRV RNase H domain is folded as a short helix and an adjacent highly bent loop. Structural superposition and subsequent mutagenesis experiments suggest that the basic protrusion motif plays a role in direct binding to the major groove in RNA/DNA hybrid, as well as in establishing the co-ordination among modules in RT necessary for proper function.

SUBMITTER: Kim JH 

PROVIDER: S-EPMC3475449 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H.

Kim Ju Hee JH   Kang Sunghyun S   Jung Suk-Kyeong SK   Yu Keum Ran KR   Chung Sang J SJ   Chung Bong Hyun BH   Erikson Raymond L RL   Kim Bo Yeon BY   Kim Seung Jun SJ  

Bioscience reports 20121001 5


RNase H (retroviral ribonuclease H) cleaves the phosphate backbone of the RNA template within an RNA/DNA hybrid to complete the synthesis of double-stranded viral DNA. In the present study we have determined the complete structure of the RNase H domain from XMRV (xenotropic murine leukaemia virus-related virus) RT (reverse transcriptase). The basic protrusion motif of the XMRV RNase H domain is folded as a short helix and an adjacent highly bent loop. Structural superposition and subsequent muta  ...[more]

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