Crystal Structures at 2.5 Angstrom Resolution of Seryl-tRNA Synthetase Complexed with Two Analogs of Seryl Adenylate
| Autor: | Michael Tukalo, Carmen Berthet-Colominas, Stephen Cusack, Mogens S. Lehmann, Gerhard Grübel, Hassan Belrhali, Anna Yaremchuk, Reuben Leberman, Barbro Beijer, Jean-Francois Legrand, Kjeld Larsen, Brian S. Sproat, Jens Aage Als-Nielsen |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Serine-tRNA Ligase Adenosine monophosphate Adenosine Protein Conformation Stereochemistry Molecular Sequence Data Beta sheet Crystallography X-Ray Protein Structure Secondary Serine chemistry.chemical_compound Computer Graphics medicine Amino Acid Sequence chemistry.chemical_classification DNA ligase Binding Sites Multidisciplinary biology Thermus thermophilus Hydrogen Bonding biology.organism_classification Adenosine Monophosphate chemistry Serine—tRNA ligase Sequence Alignment Adenosine triphosphate medicine.drug |
| Zdroj: | Science. 263:1432-1436 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.8128224 |
| Popis: | Crystal structures of seryl-tRNA synthetase from Thermus thermophilus complexed with two different analogs of seryl adenylate have been determined at 2.5 A resolution. The first complex is between the enzyme and seryl-hydroxamate-AMP (adenosine monophosphate), produced enzymatically in the crystal from adenosine triphosphate (ATP) and serine hydroxamate, and the second is with a synthetic analog of seryl adenylate (5'-O-[N-(L-seryl)-sulfamoyl]adenosine), which is a strong inhibitor of the enzyme. Both molecules are bound in a similar fashion by a network of hydrogen bond interactions in a deep hydrophilic cleft formed by the antiparallel beta sheet and surrounding loops of the synthetase catalytic domain. Four regions in the primary sequence are involved in the interactions, including the motif 2 and 3 regions of class 2 synthetases. Apart from the specific recognition of the serine side chain, the interactions are likely to be similar in all class 2 synthetases. |
| Databáze: | OpenAIRE |
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