1r0v

Structure Determination of the Dimeric Endonuclease in a Pseudo-face-centerd P21212 space group

spinqualitylabelsall models 1r0v, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r0v is a 4 chain structure with sequence from Arcfu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1r11 Gene: ENDA (ARCFU) Activity: tRNA-intron endonuclease, with EC number 3.1.27.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ENDA_ARCFU] Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp. 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 RNA-splicing endonuclease is responsible for the excision of introns in transfer RNA and archaeal ribosomal RNAs. The archaeal form of the enzyme recognizes a unique RNA motif that consists of two three-nucleotide bulges separated by a four base-paired helix, known as the bulge-helix-bulge (BHB) motif. A crystal structure of the RNA-splicing endonuclease from Archaeoglobus fulgidus (AF) has been reported previously at 2.8 A. A truncated but fully active form of AF endonuclease that lacks the N-terminal domain was expressed and crystallized in an orthorhombic space group with two dimers in the asymmetric unit. The calculated native Patterson map suggests strong pseudo-face-centering characteristics, which lead to incorrect space-group assignment by the autoindexing program. The correct space group was determined to be P2(1)2(1)2 after reindexing. The structure was solved using molecular replacement and was refined to 2.0 A. The truncated AF endonuclease structure is essentially identical to the corresponding portion of the wild-type AF endonuclease structure in space group P4(3)2(1)2 as reported previously, with the exception of loop L9, which differs owing to different crystallographic packing. These results confirm the previously described structural features of dimeric splicing endonuclease. Structure determination of a truncated dimeric splicing endonuclease in pseudo-face-centered space group P2(1)2(1)2.,Zhang Y, Li H Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):447-52. Epub 2004, Feb 25. PMID:14993668 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Endonuclease

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