1A8H

METHIONYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

Summary for 1A8H

• Entry DOI: 10.2210/pdb1a8h/pdb
• Descriptor: METHIONYL-TRNA SYNTHETASE, ZINC ION (3 entities in total)
• Functional Keywords: aminoacyl-trna synthetase, rossmann fold, riken structural genomics/proteomics initiative, rsgi, structural genomics
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: P23395
• Total number of polymer chains: 1
• Total formula weight: 58085.85

Authors

Sugiura, I.,Nureki, O.,Ugaji, Y.,Kuwabara, S.,Lober, B.,Giege, R.,Moras, D.,Yokoyama, S.,Konno, M.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 1998-03-26, release date: 1999-05-04, Last modification date: 2024-02-07)

Primary citation

Sugiura, I.,Nureki, O.,Ugaji-Yoshikawa, Y.,Kuwabara, S.,Shimada, A.,Tateno, M.,Lorber, B.,Giege, R.,Moras, D.,Yokoyama, S.,Konno, M.
The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.
Structure, 8:197-208, 2000

PubMed Abstract: The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold, which is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses, a, b and c, according to sequence homology. No conserved structural features for tRNA recognition by class I synthetases have been established.

PubMed: 10673435
DOI: 10.1016/S0969-2126(00)00095-2

Experimental method

X-RAY DIFFRACTION (2 Å)