1ZZN

Crystal structure of a group I intron/two exon complex that includes all catalytic metal ion ligands.

Summary for 1ZZN

• Entry DOI: 10.2210/pdb1zzn/pdb
• Related: 1U6B
• Descriptor: 197-MER, 5'-R(*AP*AP*GP*CP*CP*AP*CP*AP*CP*AP*AP*AP*CP*CP*AP*GP*AP*CP*GP*GP*CP*C)-3', 5'-R(*CP*AP*(5MU))-3', ... (7 entities in total)
• Functional Keywords: rna structure, ribozyme, self-splicing intron, azoarcus, two-metal-ion mechanism, structural protein-rna complex, structural protein/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P09012
• Total number of polymer chains: 4
• Total formula weight: 83512.94

Authors

Stahley, M.R.,Strobel, S.A. (deposition date: 2005-06-14, release date: 2005-08-30, Last modification date: 2023-08-23)

Primary citation

Stahley, M.R.,Strobel, S.A.
Structural evidence for a two-metal-ion mechanism of group I intron splicing.
Science, 309:1587-1590, 2005

PubMed Abstract: We report the 3.4 angstrom crystal structure of a catalytically active group I intron splicing intermediate containing the complete intron, both exons, the scissile phosphate, and all of the functional groups implicated in catalytic metal ion coordination, including the 2'-OH of the terminal guanosine. This structure suggests that, like protein phosphoryltransferases, an RNA phosphoryltransferase can use a two-metal-ion mechanism. Two Mg2+ ions are positioned 3.9 angstroms apart and are directly coordinated by all six of the biochemically predicted ligands. The evolutionary convergence of RNA and protein active sites on the same inorganic architecture highlights the intrinsic chemical capacity of the two-metal-ion catalytic mechanism for phosphoryl transfer.

PubMed: 16141079
DOI: 10.1126/science.1114994

Experimental method

X-RAY DIFFRACTION (3.37 Å)