Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H.
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.
Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Yuseong-Gu, Daejeon, Republic of Korea.
Ju Hee
JH
Kim
Sunghyun
S
Kang
Suk-Kyeong
SK
Jung
Keum Ran
KR
Yu
Sang J
SJ
Chung
Bong Hyun
BH
Chung
Raymond L
RL
Erikson
Bo Yeon
BY
Kim
Seung Jun
SJ
Kim
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012194:RNA-Directed DNA Polymerase / Q000737:chemistry / Q000378:metabolism; D016914:Ribonuclease H / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D058008:Xenotropic murine leukemia virus-related virus / Q000201:enzymology*
D012194:RNA-Directed DNA Polymerase; D016914:Ribonuclease H