1r11
From Proteopedia
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Structure Determination of the Dimeric Endonuclease in a Pseudo-face-centerd P21 space group
Overview
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.
About this Structure
1R11 is a Single protein structure of sequence from Archaeoglobus fulgidus. Active as tRNA-intron endonuclease, with EC number 3.1.27.9 Full crystallographic information is available from OCA.
Reference
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
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