論文 - 詳細
| RRC ID | 31850 |
|---|---|
| 著者 | Kobayashi K, Suzuki T, Dohmae N, Ishitani R, Nureki O. |
| タイトル | Crystallization and preliminary X-ray crystallographic analysis of YfcM: an important factor for EF-P hydroxylation. |
| ジャーナル | Acta Crystallogr F Struct Biol Commun |
| Abstract |
Elongation factor P (EF-P) plays an essential role in the translation of polyproline-containing proteins in bacteria. It becomes functional by the post-translational modification of its highly conserved lysine residue. It is first β-lysylated by PoxA and then hydroxylated by YfcM. In this work, the YfcM protein from Escherichia coli was overexpressed, purified and crystallized. The crystal of YfcM was obtained by the in situ proteolysis crystallization method and diffracted X-rays to 1.45 Å resolution. It belonged to space group C2, with unit-cell parameters a = 124.4, b = 37.0, c = 37.6 Å, β = 101.2°. The calculated Matthews coefficient (VM) of the crystal was 1.91 Å(3) Da(-1), indicating that one YfcM molecule is present in the asymmetric unit with a solvent content of 35.7%. |
| 巻・号 | 70(Pt 9) |
| ページ | 1236-9 |
| 公開日 | 2014-9-1 |
| DOI | 10.1107/S2053230X14015726 |
| PII | S2053230X14015726 |
| PMID | 25195899 |
| PMC | PMC4157426 |
| MeSH | Amino Acid Sequence Base Sequence Crystallization Crystallography, X-Ray / methods* DNA Primers Escherichia coli Proteins / chemistry* Hydroxylation Mixed Function Oxygenases / chemistry* Molecular Sequence Data Peptide Elongation Factors / chemistry* Protein Conformation Proteolysis |
| IF | 0.968 |
| 引用数 | 3 |
| WOS 分野 | CRYSTALLOGRAPHY BIOCHEMICAL RESEARCH METHODS BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 1 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 遺伝子材料 | Genomic DNA of Escherichia coli JCM 20135 (JGD07547) |
| 一般微生物 | |