2YX0

Crystal structure of P. horikoshii TYW1

Summary for 2YX0

• Entry DOI: 10.2210/pdb2yx0/pdb
• Descriptor: radical sam enzyme (2 entities in total)
• Functional Keywords: radical sam enzyme, predicted trna modification enzyme, metal binding protein, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Pyrococcus horikoshii
• Cellular location: Cytoplasm (Potential): O59412
• Total number of polymer chains: 1
• Total formula weight: 39899.39

Authors

Goto-Ito, S.,Ishii, R.,Ito, T.,Shibata, R.,Fusatomi, E.,Sekine, S.,Bessho, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-04-23, release date: 2007-10-30, Last modification date: 2024-10-30)

Primary citation

Goto-Ito, S.,Ishii, R.,Ito, T.,Shibata, R.,Fusatomi, E.,Sekine, S.,Bessho, Y.,Yokoyama, S.
Structure of an archaeal TYW1, the enzyme catalyzing the second step of wye-base biosynthesis
Acta Crystallogr.,Sect.D, 63:1059-1068, 2007

PubMed Abstract: Wye bases are tricyclic bases that are found in archaeal and eukaryotic tRNAs. The most modified wye base, wybutosine, which appears at position 37 (the 3'-adjacent position to the anticodon), is known to be important for translational reading-frame maintenance. Saccharomyces cerevisiae TYW1 catalyzes the tri-ring-formation step in wye-base biosynthesis, with the substrate tRNA bearing N(1)-methylated G37. Here, the crystal structure of the archaeal TYW1 homologue from Pyrococcus horikoshii is reported at 2.2 A resolution. The amino-acid sequence of P. horikoshii TYW1 suggested that it is a radical-AdoMet enzyme and the tertiary structure of P. horikoshii TYW1 indeed shares the modified TIM-barrel structure found in other radical-AdoMet enzymes. Radical-AdoMet enzymes generally contain one or two iron-sulfur (FeS) clusters. The tertiary structure of P. horikoshii TYW1 revealed two FeS cluster sites, each containing three cysteine residues. One FeS cluster site was expected from the amino-acid sequence and the other involves cysteine residues that are dispersed throughout the sequence. The existence of two FeS clusters was confirmed from the anomalous Fourier electron-density map. By superposing the P. horikoshii TYW1 tertiary structure on those of other radical-AdoMet enzymes, the AdoMet molecule, which is necessary for the reactions of radical-AdoMet enzymes, was modelled in P. horikoshii TYW1. Surface plots of conservation rates and electrostatic potentials revealed the highly conserved and positively charged active-site hollow. On the basis of the surface properties, a docking model of P. horikoshii TYW1, the tRNA, the FeS clusters and the AdoMet molecule was constructed, with the nucleoside at position 37 of tRNA flipped out from the canonical tRNA structure.

PubMed: 17881823
DOI: 10.1107/S0907444907040668

Experimental method

X-RAY DIFFRACTION (2.21 Å)