| http://purl.uniprot.org/citations/23275158 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23275158 | http://www.w3.org/2000/01/rdf-schema#comment | "Structures of Methanosarcina mazei pyrrolysyl-tRNA synthetase (PylRS) have been determined in a novel crystal form. The triclinic form crystals contained two PylRS dimers (four monomer molecules) in the asymmetric unit, in which the two subunits in one dimer each bind N(ℇ)-(tert-butyloxycarbonyl)-L-lysyladenylate (BocLys-AMP) and the two subunits in the other dimer each bind AMP. The BocLys-AMP molecules adopt a curved conformation and the C(α) position of BocLys-AMP protrudes from the active site. The β7-β8 hairpin structures in the four PylRS molecules represent distinct conformations of different states of the aminoacyl-tRNA synthesis reaction. Tyr384, at the tip of the β7-β8 hairpin, moves from the edge to the inside of the active-site pocket and adopts multiple conformations in each state. Furthermore, a new crystal structure of the BocLys-AMPPNP-bound form is also reported. The bound BocLys adopts an unusually bent conformation, which differs from the previously reported structure. It is suggested that the present BocLys-AMPPNP-bound, BocLys-AMP-bound and AMP-bound complexes represent the initial binding of an amino acid (or pre-aminoacyl-AMP synthesis), pre-aminoacyl-tRNA synthesis and post-aminoacyl-tRNA synthesis states, respectively. The conformational changes of Asn346 that accompany the aminoacyl-tRNA synthesis reaction have been captured by X-ray crystallographic analyses. The orientation of the Asn346 side chain, which hydrogen-bonds to the carbonyl group of the amino-acid substrate, shifts by a maximum of 85-90° around the C(β) atom."xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://purl.org/dc/terms/identifier | "doi:10.1107/s0907444912039881"xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://purl.uniprot.org/core/author | "Yokoyama S."xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://purl.uniprot.org/core/author | "Ishii R."xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://purl.uniprot.org/core/author | "Yanagisawa T."xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://purl.uniprot.org/core/author | "Sumida T."xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23275158 | http://purl.uniprot.org/core/name | "Acta Crystallogr D Biol Crystallogr"xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://purl.uniprot.org/core/pages | "5-15"xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://purl.uniprot.org/core/title | "A novel crystal form of pyrrolysyl-tRNA synthetase reveals the pre- and post-aminoacyl-tRNA synthesis conformational states of the adenylate and aminoacyl moieties and an asparagine residue in the catalytic site."xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://purl.uniprot.org/core/volume | "69"xsd:string |
| http://purl.uniprot.org/citations/23275158 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23275158 |
| http://purl.uniprot.org/citations/23275158 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23275158 |
| http://purl.uniprot.org/uniprot/#_Q8PWY1-mappedCitation-23275158 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23275158 |
| http://purl.uniprot.org/uniprot/Q8PWY1 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/23275158 |