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1P8K

The structure and DNA recognition of a bifunctional homing endonuclease and group I intron splicing factor

Summary for 1P8K
Entry DOI10.2210/pdb1p8k/pdb
Descriptor5'-D(P*GP*CP*GP*CP*GP*CP*TP*GP*AP*GP*GP*AP*GP*GP*TP*TP*TP*C)-3', 5'-D(P*TP*CP*TP*GP*TP*AP*AP*AP*GP*CP*GP*CP*A)-3', 5'-D(P*GP*CP*GP*CP*TP*TP*TP*AP*CP*AP*GP*AP*GP*AP*AP*A)-3', ... (6 entities in total)
Functional Keywordshydrolase/dna, hydrolase-dna complex
Biological sourceEmericella nidulans
Cellular locationMitochondrion: P03880
Total number of polymer chains5
Total formula weight48641.10
Authors
Stoddard, B.L.,Bolduc, J.M. (deposition date: 2003-05-07, release date: 2004-01-20, Last modification date: 2011-07-13)
Primary citationBolduc, J.M.,Spiegel, P.C.,Chatterjee, P.,Brady, K.L.,Downing, M.E.,Caprara, M.G.,Waring, R.B.,Stoddard, B.L.
Structural and biochemical analyses of DNA and RNA binding by a bifunctional homing endonuclease and group I intron splicing factor.
Genes Dev., 17:2875-2888, 2003
Cited by
PubMed Abstract: 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.
PubMed: 14633971
DOI: 10.1101/gad.1109003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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