Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome

Tateki Suzuki; Keitaro Yamashita; Yoshikazu Tanaka; Isao Tanaka; Min Yao

doi:10.1107/S2053230X14007274

Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome

Tateki Suzuki, Keitaro Yamashita, Yoshikazu Tanaka, Isao Tanaka, Min Yao

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Most canonical aminoacyl-tRNAs are synthesized directly by their cognate aminoacyl-tRNA synthetases (aaRSs), but glutaminyl-tRNA^Gln and asparaginyl-tRNA^Asn are synthesized indirectly by two-step processes. These processes are catalyzed by the transamidosome, a large ribonucleoprotein particle composed of GatA, GatB, GatC, aaRS and tRNA. In this study, the Asn-transamidosome from Pseudomonas aeruginosa was reconstructed and crystallized by mixing purified GatCAB complex, AspRS and tRNA^Asn. The crystal of the Asn-transamidosome belonged to space group P21, with unit-cell parameters a = 93.3, b = 186.0, c = 287.8 Å, β = 93.3°, and diffracted to 3.73 Å resolution. Preliminary X-ray crystallographic analysis showed that the asymmetric unit contained two Asn-transamidosomes, each composed of two GatCABs, one AspRS dimer and two tRNA^Asns, indicating that the construction of the current Asn-transamidosome differs from that of Thermus thermophilus.

Original language	English
Pages (from-to)	790-793
Number of pages	4
Journal	Acta Crystallographica Section F:Structural Biology Communications
Volume	70
Issue number	6
DOIs	https://doi.org/10.1107/S2053230X14007274
Publication status	Published - Jun 2014
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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title = "Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome",

abstract = "Most canonical aminoacyl-tRNAs are synthesized directly by their cognate aminoacyl-tRNA synthetases (aaRSs), but glutaminyl-tRNAGln and asparaginyl-tRNAAsn are synthesized indirectly by two-step processes. These processes are catalyzed by the transamidosome, a large ribonucleoprotein particle composed of GatA, GatB, GatC, aaRS and tRNA. In this study, the Asn-transamidosome from Pseudomonas aeruginosa was reconstructed and crystallized by mixing purified GatCAB complex, AspRS and tRNAAsn. The crystal of the Asn-transamidosome belonged to space group P21, with unit-cell parameters a = 93.3, b = 186.0, c = 287.8 {\AA}, β = 93.3°, and diffracted to 3.73 {\AA} resolution. Preliminary X-ray crystallographic analysis showed that the asymmetric unit contained two Asn-transamidosomes, each composed of two GatCABs, one AspRS dimer and two tRNAAsns, indicating that the construction of the current Asn-transamidosome differs from that of Thermus thermophilus.",

author = "Tateki Suzuki and Keitaro Yamashita and Yoshikazu Tanaka and Isao Tanaka and Min Yao",

year = "2014",

month = jun,

doi = "10.1107/S2053230X14007274",

language = "English",

volume = "70",

pages = "790--793",

journal = "Acta Crystallographica Section F:Structural Biology Communications",

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T1 - Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome

AU - Suzuki, Tateki

AU - Yamashita, Keitaro

AU - Tanaka, Yoshikazu

AU - Tanaka, Isao

AU - Yao, Min

PY - 2014/6

Y1 - 2014/6

N2 - Most canonical aminoacyl-tRNAs are synthesized directly by their cognate aminoacyl-tRNA synthetases (aaRSs), but glutaminyl-tRNAGln and asparaginyl-tRNAAsn are synthesized indirectly by two-step processes. These processes are catalyzed by the transamidosome, a large ribonucleoprotein particle composed of GatA, GatB, GatC, aaRS and tRNA. In this study, the Asn-transamidosome from Pseudomonas aeruginosa was reconstructed and crystallized by mixing purified GatCAB complex, AspRS and tRNAAsn. The crystal of the Asn-transamidosome belonged to space group P21, with unit-cell parameters a = 93.3, b = 186.0, c = 287.8 Å, β = 93.3°, and diffracted to 3.73 Å resolution. Preliminary X-ray crystallographic analysis showed that the asymmetric unit contained two Asn-transamidosomes, each composed of two GatCABs, one AspRS dimer and two tRNAAsns, indicating that the construction of the current Asn-transamidosome differs from that of Thermus thermophilus.

AB - Most canonical aminoacyl-tRNAs are synthesized directly by their cognate aminoacyl-tRNA synthetases (aaRSs), but glutaminyl-tRNAGln and asparaginyl-tRNAAsn are synthesized indirectly by two-step processes. These processes are catalyzed by the transamidosome, a large ribonucleoprotein particle composed of GatA, GatB, GatC, aaRS and tRNA. In this study, the Asn-transamidosome from Pseudomonas aeruginosa was reconstructed and crystallized by mixing purified GatCAB complex, AspRS and tRNAAsn. The crystal of the Asn-transamidosome belonged to space group P21, with unit-cell parameters a = 93.3, b = 186.0, c = 287.8 Å, β = 93.3°, and diffracted to 3.73 Å resolution. Preliminary X-ray crystallographic analysis showed that the asymmetric unit contained two Asn-transamidosomes, each composed of two GatCABs, one AspRS dimer and two tRNAAsns, indicating that the construction of the current Asn-transamidosome differs from that of Thermus thermophilus.

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Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome

Abstract

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