4E51

Crystal structure of a histidyl-tRNA synthetase HisRS from Burkholderia thailandensis bound to histidine

Summary for 4E51

• Entry DOI: 10.2210/pdb4e51/pdb
• Descriptor: Histidine--tRNA ligase, HISTIDINE (3 entities in total)
• Functional Keywords: seattle structural genomics center for infectious disease, ssgcid, aminoacylation, trna activation, charged trna, histidyl-adenylate, atp-dependent, ligase, trna synthetase, aars
• Biological source: Burkholderia thailandensis
• Cellular location: Cytoplasm : Q2SWE3
• Total number of polymer chains: 2
• Total formula weight: 104187.57

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2012-03-13, release date: 2012-03-28, Last modification date: 2023-09-13)

Primary citation

Moen, S.O.,Edwards, T.E.,Dranow, D.M.,Clifton, M.C.,Sankaran, B.,Van Voorhis, W.C.,Sharma, A.,Manoil, C.,Staker, B.L.,Myler, P.J.,Lorimer, D.D.
Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms.
Sci Rep, 7:223-223, 2017

PubMed Abstract: Aminoacyl-tRNA synthetases (aaRSs) charge tRNAs with their cognate amino acid, an essential precursor step to loading of charged tRNAs onto the ribosome and addition of the amino acid to the growing polypeptide chain during protein synthesis. Because of this important biological function, aminoacyl-tRNA synthetases have been the focus of anti-infective drug development efforts and two aaRS inhibitors have been approved as drugs. Several researchers in the scientific community requested aminoacyl-tRNA synthetases to be targeted in the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure determination pipeline. Here we investigate thirty-one aminoacyl-tRNA synthetases from infectious disease organisms by co-crystallization in the presence of their cognate amino acid, ATP, and/or inhibitors. Crystal structures were determined for a CysRS from Borrelia burgdorferi bound to AMP, GluRS from Borrelia burgdorferi and Burkholderia thailandensis bound to glutamic acid, a TrpRS from the eukaryotic pathogen Encephalitozoon cuniculi bound to tryptophan, a HisRS from Burkholderia thailandensis bound to histidine, and a LysRS from Burkholderia thailandensis bound to lysine. Thus, the presence of ligands may promote aaRS crystallization and structure determination. Comparison with homologous structures shows conformational flexibility that appears to be a recurring theme with this enzyme class.

PubMed: 28303005
DOI: 10.1038/s41598-017-00367-6

Experimental method

X-RAY DIFFRACTION (2.65 Å)