4E89

Crystal Structure of RnaseH from gammaretrovirus

Summary for 4E89

• Entry DOI: 10.2210/pdb4e89/pdb
• Descriptor: RNase H, CADMIUM ION, MAGNESIUM ION (3 entities in total)
• Functional Keywords: rossmann fold, hydrolase
• Biological source: Xenotropic MuLV-related virus (XMRV)
• Cellular location: Gag-Pol polyprotein: Host cell membrane; Lipid-anchor (Potential). Matrix protein p15: Virion (Potential). Capsid protein p30: Virion (Potential). Nucleocapsid protein p10: Virion (Potential): A1Z651
• Total number of polymer chains: 1
• Total formula weight: 17778.56

Authors

Kim, J.H.,Kim, S.J. (deposition date: 2012-03-19, release date: 2012-10-17, Last modification date: 2024-03-20)

Primary citation

Kim, J.H.,Kang, S.,Jung, S.K.,Yu, K.R.,Chung, S.J.,Chung, B.H.,Erikson, R.L.,Kim, B.Y.,Kim, S.J.
Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H
Biosci.Rep., 32:455-463, 2012

PubMed 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.

PubMed: 22724525
DOI: 10.1042/BSR20120028

Experimental method

X-RAY DIFFRACTION (2.6 Å)