Purification, crystallization and preliminary X-ray characterization of a human mitochondrial phenylalanyl-tRNA synthetase
| Autor: | Nina Moor, Emine C. Koc, Mark Safro, Liron Klipcan, Paul D. Templeton, Naama Kessler, Linda L. Spremulli, Inna Levin |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Phenylalanine
Biophysics Aminoacylation Mitochondrion Biochemistry law.invention Phenylalanine—tRNA ligase Adenosine Triphosphate X-Ray Diffraction Structural Biology law Genetics Humans chemistry.chemical_classification Condensed Matter Physics Amino acid Mitochondria Enzyme chemistry Crystallization Communications Transfer RNA Recombinant DNA Electrophoresis Polyacrylamide Gel Phenylalanine-tRNA Ligase Crystallization |
| DOI: | 10.17615/awg4-mb51 |
| Popis: | Human monomeric mitochondrial phenylalanyl-tRNA synthetase (mitPheRS) is an enzyme that catalyzes the charging of tRNA with the cognate amino acid phenylalanine. Human mitPheRS is a chimera of the bacterial alpha-subunit of PheRS and the B8 domain of its beta-subunit. Together, the alpha-subunit and the 'RNP-domain' (B8 domain) at the C-terminus form the minimal structural set to construct an enzyme with phenylalanylation activity. The recombinant human mitPheRS was purified to homogeneity and crystallized in complex with phenylalanine and ATP. The crystals diffracted to 2.2 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 55, b = 90, c = 96 A. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|