2AB5

bI3 LAGLIDADG Maturase

Summary for 2AB5

• Entry DOI: 10.2210/pdb2ab5/pdb
• Descriptor: mRNA maturase, SULFATE ION (3 entities in total)
• Functional Keywords: maturase, laglidadg endonuclease, group i intron splicing, rna binding, protein binding
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 66243.90

Authors

Longo, A.,Leonard, C.W.,Bassi, G.S.,Berndt, D.,Krahn, J.M.,Hall, T.M.,Weeks, K.M. (deposition date: 2005-07-14, release date: 2005-08-30, Last modification date: 2024-10-30)

Primary citation

Longo, A.,Leonard, C.W.,Bassi, G.S.,Berndt, D.,Krahn, J.M.,Hall, T.M.,Weeks, K.M.
Evolution from DNA to RNA recognition by the bI3 LAGLIDADG maturase
Nat.Struct.Mol.Biol., 12:779-787, 2005

PubMed Abstract: LAGLIDADG endonucleases bind across adjacent major grooves via a saddle-shaped surface and catalyze DNA cleavage. Some LAGLIDADG proteins, called maturases, facilitate splicing by group I introns, raising the issue of how a DNA-binding protein and an RNA have evolved to function together. In this report, crystallographic analysis shows that the global architecture of the bI3 maturase is unchanged from its DNA-binding homologs; in contrast, the endonuclease active site, dispensable for splicing facilitation, is efficiently compromised by a lysine residue replacing essential catalytic groups. Biochemical experiments show that the maturase binds a peripheral RNA domain 50 A from the splicing active site, exemplifying long-distance structural communication in a ribonucleoprotein complex. The bI3 maturase nucleic acid recognition saddle interacts at the RNA minor groove; thus, evolution from DNA to RNA function has been mediated by a switch from major to minor groove interaction.

PubMed: 16116439
DOI: 10.1038/nsmb976

Experimental method

X-RAY DIFFRACTION (2.2 Å)