1OBH
LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A PRE-TRANSFER EDITING SUBSTRATE ANALOGUE IN BOTH SYNTHETIC ACTIVE SITE AND EDITING SITE
Summary for 1OBH
| Entry DOI | 10.2210/pdb1obh/pdb |
| Related | 1H3N 1JZQ 1JZS 1OBC |
| Descriptor | LEUCYL-TRNA SYNTHETASE, SULFATE ION, MERCURY (II) ION, ... (6 entities in total) |
| Functional Keywords | synthetase, aminoacyl-trna synthetase, class i aminoacyl-trna synthetase, atp + l-leucine + trna (leu) -> amp + ppi l- leucyl-trna(leu) |
| Biological source | THERMUS THERMOPHILUS |
| Total number of polymer chains | 1 |
| Total formula weight | 102874.05 |
| Authors | Cusack, S.,Yaremchuk, A.,Tukalo, M. (deposition date: 2003-01-31, release date: 2003-05-09, Last modification date: 2024-11-20) |
| Primary citation | Lincecum, T.,Tukalo, M.,Yaremchuk, A.,Mursinna, R.,Williams, A.,Sproat, B.,Van Den Eynde, W.,Link, A.,Van Calenbergh, S.,Grotli, M.,Martinis, S.,Cusack, S. Structural and Mechanistic Basis of Pre- and Posttransfer Editing by Leucyl-tRNA Synthetase Mol.Cell, 11:951-, 2003 Cited by PubMed Abstract: The aminoacyl-tRNA synthetases link tRNAs with their cognate amino acid. In some cases, their fidelity relies on hydrolytic editing that destroys incorrectly activated amino acids or mischarged tRNAs. We present structures of leucyl-tRNA synthetase complexed with analogs of the distinct pre- and posttransfer editing substrates. The editing active site binds the two different substrates using a single amino acid discriminatory pocket while preserving the same mode of adenine recognition. This suggests a similar mechanism of hydrolysis for both editing substrates that depends on a key, completely conserved aspartic acid, which interacts with the alpha-amino group of the noncognate amino acid and positions both substrates for hydrolysis. Our results demonstrate the economy by which a single active site accommodates two distinct substrates in a proofreading process critical to the fidelity of protein synthesis. PubMed: 12718881DOI: 10.1016/S1097-2765(03)00098-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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