1R11

Structure Determination of the Dimeric Endonuclease in a Pseudo-face-centerd P21 space group

Summary for 1R11

• Entry DOI: 10.2210/pdb1r11/pdb
• Related: 1R0V
• Descriptor: tRNA-intron endonuclease (1 entity in total)
• Functional Keywords: rna splicing; endonuclease; x-ray crystallography, translation, hydrolase
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 2
• Total formula weight: 72000.47

Authors

Li, H.,Zhang, Y. (deposition date: 2003-09-23, release date: 2004-03-09, Last modification date: 2024-02-14)

Primary citation

Zhang, Y.,Li, H.
Structure determination of a truncated dimeric splicing endonuclease in pseudo-face-centered space group P2(1)2(1)2.
Acta Crystallogr.,Sect.D, 60:447-452, 2004

PubMed Abstract: 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.

PubMed: 14993668
DOI: 10.1107/S0907444903029482

Experimental method

X-RAY DIFFRACTION (2.7 Å)