3p83 | pdb_00003p83

Structure of the PCNA:RNase HII complex from Archaeoglobus fulgidus.

spinqualitylabelsall models 3p83, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3p83 is a 6 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1i39, 1rxm Gene: pcn, AF_0335 (ARCFL), AF_0621, rnhB (ARCFL) Activity: Ribonuclease H, with EC number 3.1.26.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PCNA_ARCFU] Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication (By similarity). [RNH2_ARCFU] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (By similarity).[HAMAP-Rule:MF_00052_A] Publication Abstract from PubMed Ribonuclease H2 is the major nuclear enzyme degrading cellular RNA/DNA hybrids in eukaryotes and the sole nuclease known to be able to hydrolyze ribonucleotides misincorporated during genomic replication. Mutation in RNASEH2 causes Aicardi-Goutieres syndrome, an auto-inflammatory disorder that may arise from nucleic acid byproducts generated during DNA replication. Here, we report the crystal structures of Archaeoglobus fulgidus RNase HII in complex with PCNA, and human PCNA bound to a C-terminal peptide of RNASEH2B. In the archaeal structure, three binding modes are observed as the enzyme rotates about a flexible hinge while anchored to PCNA by its PIP-box motif. PCNA binding promotes RNase HII activity in a hinge-dependent manner. It enhances both cleavage of ribonucleotides misincorporated in DNA duplexes, and the comprehensive hydrolysis of RNA primers formed during Okazaki fragment maturation. In addition, PCNA imposes strand specificity on enzyme function, and by localizing RNase H2 and not RNase H1 to nuclear replication foci in vivo it ensures that RNase H2 is the dominant RNase H activity during nuclear replication. Our findings provide insights into how type 2 RNase H activity is directed during genome replication and repair, and suggest a mechanism by which RNase H2 may suppress generation of immunostimulatory nucleic acids. PCNA directs type 2 RNase H activity on DNA replication and repair substrates.,Bubeck D, Reijns MA, Graham SC, Astell KR, Jones EY, Jackson AP Nucleic Acids Res. 2011 Jan 17. PMID:21245041 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proliferating Cell Nuclear Antigen Ribonuclease Temp

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