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Structure of a tryptophanyl-tRNA synthetase containing an iron–sulfur cluster

Journal Article · · Acta Crystallographica. Section F
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  1. The Scripps Research Inst., La Jolla, CA (United States); DOE/OSTI
  2. The Scripps Research Inst., La Jolla, CA (United States)
  3. The Scripps Research Inst., La Jolla, CA (United States); Genomics Inst. of the Novartis Research Foundation, San Diego, CA (United States)
  4. The Scripps Research Inst., La Jolla, CA (United States); Univ. of California, San Diego, La Jolla, CA (United States); Sanford–Burnham Medical Research Inst., La Jolla, CA (United States)
  5. The Scripps Research Inst., La Jolla, CA (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
  6. The Scripps Research Inst., La Jolla, CA (United States); Sanford–Burnham Medical Research Inst., La Jolla, CA (United States)
  7. Genomics Inst. of the Novartis Research Foundation, San Diego, CA (United States)
  8. The Scripps Research Inst., La Jolla, CA (United States); Univ. of California, San Diego, La Jolla, CA (United States)
  9. The Scripps Research Inst., La Jolla, CA (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States)
A novel aminoacyl-tRNA synthetase that contains an iron–sulfur cluster in the tRNA anticodon-binding region and efficiently charges tRNA with tryptophan has been found in Thermotoga maritima. The crystal structure of TmTrpRS (tryptophanyl-tRNA synthetase; TrpRS; EC 6.1.1.2) reveals an iron–sulfur [4Fe–4S] cluster bound to the tRNA anticodon-binding (TAB) domain and an l-tryptophan ligand in the active site. None of the other T. maritima aminoacyltRNA synthetases (AARSs) contain this [4Fe–4S] cluster-binding motif (C-x22- C-x6-C-x2-C). It is speculated that the iron–sulfur cluster contributes to the stability of TmTrpRS and could play a role in the recognition of the anticodon.
Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)
Sponsoring Organization:
National Center for Research Resources (NCRR); National Institute of General Medical Sciences (NIGMS); National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
Grant/Contract Number:
AC02-05CH11231
OSTI ID:
1625806
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: 10 Vol. 66; ISSN ACSFCL; ISSN 1744-3091
Publisher:
International Union of CrystallographyCopyright Statement
Country of Publication:
United States
Language:
English

Cited By (3)

The Relationship between Environmental Dioxygen and Iron-Sulfur Proteins Explored at the Genome Level journal January 2017
Can we predict the clinical outcome of arthroscopic partial meniscectomy? A systematic review journal November 2017
Bioinformatic Analysis Reveals Archaeal tRNATyr and tRNATrp Identities in Bacteria journal February 2017

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