2ZYZ
Pyrobaculum aerophilum splicing endonuclease
Summary for 2ZYZ
| Entry DOI | 10.2210/pdb2zyz/pdb |
| Descriptor | Putative uncharacterized protein PAE0789, tRNA-splicing endonuclease (3 entities in total) |
| Functional Keywords | splicing endonuclease, crenarchaea, heterotetramer, rna processing, endonuclease, hydrolase, nuclease, trna processing, splicing |
| Biological source | Pyrobaculum aerophilum More |
| Total number of polymer chains | 4 |
| Total formula weight | 68255.23 |
| Authors | Yoshinari, S.,Inaoka, D.K.,Watanabe, Y.,Shiba, T.,Kurisu, G.,Harada, S. (deposition date: 2009-01-30, release date: 2009-06-23, Last modification date: 2024-03-13) |
| Primary citation | Yoshinari, S.,Shiba, T.,Inaoka, D.K.,Itoh, T.,Kurisu, G.,Harada, S.,Kita, K.,Watanabe, Y. Functional importance of crenarchaea-specific extra-loop revealed by an X-ray structure of a heterotetrameric crenarchaeal splicing endonuclease Nucleic Acids Res., 37:4787-4798, 2009 Cited by PubMed Abstract: Archaeal splicing endonucleases (EndAs) are currently classified into three groups. Two groups require a single subunit protein to form a homodimer or homotetramer. The third group requires two nonidentical protein components for the activity. To elucidate the molecular architecture of the two-subunit EndA system, we studied a crenarchaeal splicing endonuclease from Pyrobaculum aerophilum. In the present study, we solved a crystal structure of the enzyme at 1.7-A resolution. The enzyme adopts a heterotetrameric form composed of two catalytic and two structural subunits. By connecting the structural and the catalytic subunits of the heterotetrameric EndA, we could convert the enzyme to a homodimer that maintains the broad substrate specificity that is one of the characteristics of heterotetrameric EndA. Meanwhile, a deletion of six amino acids in a Crenarchaea-specific loop abolished the endonuclease activity even on a substrate with canonical BHB motif. These results indicate that the subunit architecture is not a major factor responsible for the difference of substrate specificity between single- and two-subunit EndA systems. Rather, the structural basis for the broad substrate specificity is built into the crenarchaeal splicing endonuclease itself. PubMed: 19515941DOI: 10.1093/nar/gkp506 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
