ISDA: 1A79

Deposition Date 1998-03-23

Release Date 1999-06-01

Last Version Date 2024-02-07

Entry Detail

PDB ID:

1A79

Keywords:

ENDONUCLEASE

Title:

CRYSTAL STRUCTURE OF THE TRNA SPLICING ENDONUCLEASE FROM METHANOCOCCUS JANNASCHII

Biological Source:

Source Organism(s):

Methanocaldococcus jannaschii (Taxon ID: 2190)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.28 Å

R-Value Free:

0.26

R-Value Work:

0.20

R-Value Observed:

0.20

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:TRNA ENDONUCLEASE
Gene (Uniprot):endA
Chain IDs:A, B, C, D
Chain Length:171
Number of Molecules:4
Biological Source:Methanocaldococcus jannaschii

UniProt ID:Q58819 Pfam ID:PF02778, PF01974 EC:4.6.1.16

Ligand Molecules

SO4

Primary Citation

Crystal structure and evolution of a transfer RNA splicing enzyme.

Li, H, Trotta, C.R, Abelson, J.Show

Science 280 279 284 (1998)

PMID: 9535656 DOI: 10.1126/science.280.5361.279

Abstact

The splicing of transfer RNA precursors is similar in Eucarya and Archaea. In both kingdoms an endonuclease recognizes the splice sites and releases the intron, but the mechanism of splice site recognition is different in each kingdom. The crystal structure of the endonuclease from the archaeon Methanococcus jannaschii was determined to a resolution of 2.3 angstroms. The structure indicates that the cleavage reaction is similar to that of ribonuclease A and the arrangement of the active sites is conserved between the archaeal and eucaryal enzymes. These results suggest an evolutionary pathway for splice site recognition.

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Protein

Chemical

Disease

Primary Citation of related structures

Abstact

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