1p8k
From Proteopedia
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The structure and DNA recognition of a bifunctional homing endonuclease and group I intron splicing factor
Overview
We determined the crystal structure of a bifunctional group I intron, splicing factor and homing endonuclease, termed the I-AniI maturase, in, complex with its DNA target at 2.6 A resolution. The structure, demonstrates the remarkable structural conservation of the beta-sheet, DNA-binding motif between highly divergent enzyme subfamilies. DNA, recognition by I-AniI was further studied using nucleoside deletion and, DMS modification interference analyses. Correlation of these results with, the crystal structure provides information on the relative importance of, individual nucleotide contacts for DNA recognition. Alignment and modeling, of two homologous maturases reveals conserved basic surface residues, distant from the DNA-binding surface, that might be involved in RNA, binding. A point mutation that introduces a single negative charge in this, region uncouples the maturase and endonuclease functions of the protein, inhibiting RNA binding and splicing while maintaining DNA binding and, cleavage.
About this Structure
1P8K is a Single protein structure of sequence from Emericella nidulans with MG as ligand. Full crystallographic information is available from OCA.
Reference
Structural and biochemical analyses of DNA and RNA binding by a bifunctional homing endonuclease and group I intron splicing factor., Bolduc JM, Spiegel PC, Chatterjee P, Brady KL, Downing ME, Caprara MG, Waring RB, Stoddard BL, Genes Dev. 2003 Dec 1;17(23):2875-88. Epub 2003 Nov 21. PMID:14633971
Page seeded by OCA on Tue Nov 20 23:35:51 2007
