| http://purl.uniprot.org/citations/25817995 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25817995 | http://www.w3.org/2000/01/rdf-schema#comment | "A conserved structural module following the KMSKS catalytic loop exhibits α-α-β-α topology in class Ia and Ib aminoacyl-tRNA synthetases. However, the function of this domain has received little attention. Here, we describe the effect this module has on the aminoacylation and editing capacities of leucyl-tRNA synthetases (LeuRSs) by characterizing the key residues from various species. Mutation of highly conserved basic residues on the third α-helix of this domain impairs the affinity of LeuRS for the anticodon stem of tRNA(Leu), which decreases both aminoacylation and editing activities. Two glycine residues on this α-helix contribute to flexibility, leucine activation, and editing of LeuRS from Escherichia coli (EcLeuRS). Acidic residues on the β-strand enhance the editing activity of EcLeuRS and sense the size of the tRNA(Leu) D-loop. Incorporation of these residues stimulates the tRNA-dependent editing activity of the chimeric minimalist enzyme Mycoplasma mobile LeuRS fused to the connective polypeptide 1 editing domain and leucine-specific domain from EcLeuRS. Together, these results reveal the stem contact-fold to be a functional as well as a structural linker between the catalytic site and the tRNA binding domain. Sequence comparison of the EcLeuRS stem contact-fold domain with editing-deficient enzymes suggests that key residues of this module have evolved an adaptive strategy to follow the editing functions of LeuRS."xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m115.639492"xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/author | "Chen X."xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/author | "Tan M."xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/author | "Yan W."xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/author | "Ye Q."xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/author | "Wang E.D."xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/author | "Eriani G."xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/pages | "12256-12267"xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/title | "Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module."xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://purl.uniprot.org/core/volume | "290"xsd:string |
| http://purl.uniprot.org/citations/25817995 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25817995 |
| http://purl.uniprot.org/citations/25817995 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25817995 |
| http://purl.uniprot.org/uniprot/#_A0A6I8PL42-mappedCitation-25817995 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25817995 |
| http://purl.uniprot.org/uniprot/#_B2RCM2-mappedCitation-25817995 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25817995 |
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| http://purl.uniprot.org/uniprot/#_Q9NPU8-mappedCitation-25817995 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25817995 |
| http://purl.uniprot.org/uniprot/#_Q0VGM8-mappedCitation-25817995 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25817995 |
| http://purl.uniprot.org/uniprot/#_Q9P2J5-mappedCitation-25817995 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25817995 |
| http://purl.uniprot.org/uniprot/#_Q9HAM7-mappedCitation-25817995 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25817995 |