4e89 | pdb_00004e89

Crystal Structure of RnaseH from gammaretrovirus

spinqualitylabelsall models 4e89, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4e89 is a 1 chain structure with sequence from Xenotropic mulv-related virus vp62. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD, MG Activity: Ribonuclease H, with EC number 3.1.26.4 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H.,Kim JH, Kang S, Jung SK, Yu KR, Chung SJ, Chung BH, Erikson RL, Kim BY, Kim SJ Biosci Rep. 2012 Oct 1;32(5):455-63. PMID:22724525 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease User:Jaime.Prilusky/Test/tree

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