2qk9

Human RNase H catalytic domain mutant D210N in complex with 18-mer RNA/DNA hybrid

spinqualitylabelsall models 2qk9, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qk9 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 16D, FLC, GOL, NA, SO4 Related: 2qkb, 2qkk Gene: RNASEH1, RNH1 (Homo sapiens) Activity: Ribonuclease H, with EC number 3.1.26.4 Resources: FirstGlance, OCA, RCSB, PDBsum Function [RNH1_HUMAN] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We report here crystal structures of human RNase H1 complexed with an RNA/DNA substrate. Unlike B. halodurans RNase H1, human RNase H1 has a basic protrusion, which forms a DNA-binding channel and together with the conserved phosphate-binding pocket confers specificity for the B form and 2'-deoxy DNA. The RNA strand is recognized by four consecutive 2'-OH groups and cleaved by a two-metal ion mechanism. Although RNase H1 is overall positively charged, the substrate interface is neutral to acidic in character, which likely contributes to the catalytic specificity. Positions of the scissile phosphate and two catalytic metal ions are interdependent and highly coupled. Modeling of HIV reverse transcriptase (RT) with RNA/DNA in its RNase H active site suggests that the substrate cannot simultaneously occupy the polymerase active site and must undergo a conformational change to toggle between the two catalytic centers. The region that accommodates this conformational change offers a target to develop HIV-specific inhibitors. Structure of human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription.,Nowotny M, Gaidamakov SA, Ghirlando R, Cerritelli SM, Crouch RJ, Yang W Mol Cell. 2007 Oct 26;28(2):264-76. PMID:17964265 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease Temp User:Jaime.Prilusky/Test/tree

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