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基本情報
| 登録情報 | データベース: SASBDB / ID: SASDD53 |
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試料 | Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C
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| 機能・相同性 | 機能・相同性情報 |
| 生物種 | Enterobacter sp. CJF-002 (バクテリア) |
引用 | ジャーナル: Sci Rep / 年: 2017タイトル: Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C. 著者: Shingo Nojima / Ayumi Fujishima / Koji Kato / Kayoko Ohuchi / Nobutaka Shimizu / Kento Yonezawa / Kenji Tajima / Min Yao / ![]() 要旨: Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit ...Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a β-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24-Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra α-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted α-helix. Such structural feature indicates that the inserted α-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24-Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the α-helical hinge may play important role for exporting glucan chains. |
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構造の表示
| 構造ビューア | 分子: Molmil Jmol/JSmol |
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-モデル
| モデル #1746 | ![]() タイプ: dummy / ソフトウェア: (ATSAS 2.7) / ダミー原子の半径: 4.25 A / 対称性: P1 / カイ2乗値: 1.906 / P-value: 0.000126 Omokage検索でこの集合体の類似形状データを探す (詳細) |
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試料
試料 | 名称: Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C 試料濃度: 0.71-1.80 |
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| バッファ | 名称: 50 mM HEPES, 100 mM KCl / pH: 8 |
| 要素 #947 | 名称: BcsC-TPR / タイプ: protein / 記述: Bacterial cellulose synthesis subunit C / 分子量: 71.298 / 分子数: 1 / 由来: Enterobacter sp. CJF-002 / 参照: UniProt: K0J1W8 配列: GHMDEPTAQQ QLLSQVRLGE ATKREDLVRQ SLYRLELIDP DNPDVIAARF RYLLRQGDNA GAQKQLDRMK QLAPDSAAYK SSVTSMTLSG AEGRQALQQA RLQATTGHVP EALAAYDALF KGNPPEGDLA VEYWALVAKV PARRSEAITQ LKALNARNPG NAALQNSLAQ ...配列: GHMDEPTAQQ QLLSQVRLGE ATKREDLVRQ SLYRLELIDP DNPDVIAARF RYLLRQGDNA GAQKQLDRMK QLAPDSAAYK SSVTSMTLSG AEGRQALQQA RLQATTGHVP EALAAYDALF KGNPPEGDLA VEYWALVAKV PARRSEAITQ LKALNARNPG NAALQNSLAQ LLFGEGRDAE AYAVLEQMAK SSAGREAAAG LWYQQIQRMP VSDASVKALQ RFLTVFSSGD TVDSARTQLA AQQKQLADPA FRARATGLAA VDAGQGAKAV NELRQAVNAN GTDSEAVGAL GQAYSQSGDR ARAVAQFEKA IAMDPTSGNR SKWDSLLKTN RYWLLIQQGD AALKANNPGE AERLYSQARR IDNTDSYAVL GLGDAAMARK DSHAAESFYR QALRMDSGNS NAVRGLANIY RARSPQEADT FIQSLSASQR RSIDDIERGL KNDRLAQQAE ALENSGQWAQ AAELQRQRLA LDPGSVWVTY RLASDLRQAG EPREADAHMQ RLAALKPGDP EQVYAYGLYL SGNNQEMAAL NQLNALPKAQ WNSNIQELAE RLQTNRLLDN ANRLRDSGHE EQARALLAQQ PASTRIDLTL ADWAQQGGDS ASAQHYFNRV LEREPNNQDA LLGLAELYAA DGNKMAARAQ LAKLLEHHHH HH |
-実験情報
| ビーム | 設備名称: Photon Factory (PF), High Energy Acceleration Research Organization (KEK) BL-10C 地域: Tsukuba / 国: Japan / 線源: X-ray synchrotron / 波長: 0.1 Å / スペクトロメータ・検出器間距離: 2.01 mm | |||||||||||||||||||||||||||||||||||||||
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| 検出器 | 名称: Pilatus3 2M / Pixsize x: 0.172 mm | |||||||||||||||||||||||||||||||||||||||
| スキャン | 測定日: 2017年4月24日 / 保管温度: 20 °C / セル温度: 20 °C / 照射時間: 20 sec. / フレーム数: 28 / 単位: 1/A /
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| 距離分布関数 P(R) |
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コントローラー
万見について



Enterobacter sp. CJF-002 (バクテリア)
引用
登録者
SASDD53










