+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 2k0x | ||||||
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タイトル | The actinorhodin holo acyl carrier protein from S. coelicolor | ||||||
要素 | Actinorhodin polyketide synthase acyl carrier protein | ||||||
キーワード | TRANSPORT PROTEIN / Acyl carrier protein / polyketide / holo / phosphopantetheine / Antibiotic biosynthesis | ||||||
機能・相同性 | 機能・相同性情報 lipid A biosynthetic process / acyl binding / antibiotic biosynthetic process / acyl carrier activity / cytosol 類似検索 - 分子機能 | ||||||
生物種 | Streptomyces coelicolor (バクテリア) | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
Model details | This deposit is a set of twenty structures of the holo (phosphopantetheinylated) actinorhodin ...This deposit is a set of twenty structures of the holo (phosphopantetheinylated) actinorhodin polyketide acyl carrier protein (ACP). These datasets form a sister set to the recent apo- coordinates we deposited and can be used to directly compare the two forms. | ||||||
データ登録者 | Crump, M.P. / Evans, S.E. / Williams, C. | ||||||
引用 | ジャーナル: Chembiochem / 年: 2008 タイトル: An ACP Structural Switch: Conformational Differences between the Apo and Holo Forms of the Actinorhodin Polyketide Synthase Acyl Carrier Protein. 著者: Evans, S.E. / Williams, C. / Arthur, C.J. / Burston, S.G. / Simpson, T.J. / Crosby, J. / Crump, M.P. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 2k0x.cif.gz | 560.9 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb2k0x.ent.gz | 495.2 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 2k0x.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/k0/2k0x ftp://data.pdbj.org/pub/pdb/validation_reports/k0/2k0x | HTTPS FTP |
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-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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NMR アンサンブル |
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-要素
#1: タンパク質 | 分子量: 9239.177 Da / 分子数: 1 / 変異: C17S / 由来タイプ: 組換発現 由来: (組換発現) Streptomyces coelicolor (バクテリア) 株: A3(2) 解説: Actinorhodin acyl carrier protein (act ACP) from S. coelicolor was heterologously overexpressed in its apo form in E. coli BL21 (DE3) cells. These cells contained the plasmid pET11c C17S act ...解説: Actinorhodin acyl carrier protein (act ACP) from S. coelicolor was heterologously overexpressed in its apo form in E. coli BL21 (DE3) cells. These cells contained the plasmid pET11c C17S act ACP (courtesy of Dr. Tom Nicholson). This IPTG inducible vector is both easier to use and more reliable than the heat inducible pT7-7 version originally constructed. The protein was modified to the holo form using S. coelicolor ACPS and Enzyme CoA. 遺伝子: actI / 発現宿主: Escherichia coli (大腸菌) / 株 (発現宿主): BL21 / Variant (発現宿主): DE3 / 参照: UniProt: Q02054 |
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#2: 化合物 | ChemComp-PNS / |
-実験情報
-実験
実験 | 手法: 溶液NMR 詳細: This deposit is a set of twenty structures of the holo (phosphopantetheinylated) actinorhodin polyketide acyl carrier protein (ACP). These datasets form a sister set to the recent apo- ...詳細: This deposit is a set of twenty structures of the holo (phosphopantetheinylated) actinorhodin polyketide acyl carrier protein (ACP). These datasets form a sister set to the recent apo- coordinates we deposited and can be used to directly compare the two forms. | ||||||||||||||||||||||||||||||||||||||||||||
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NMR実験 |
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-試料調製
詳細 | 内容: 1-2 mM [U-98% 13C; U-98% 15N] act holo-acp, 1-2 mM Phosphopantetheine side chain, 95 % H2O, 5 % D2O, 20 mM potassium phosphate, 5 mM TCEP, 1 mM sodium azide, 95% H2O/5% D2O 溶媒系: 95% H2O/5% D2O | ||||||||||||||||||||||||||||||||
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試料 |
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試料状態 | pH: 5.5 / 圧: ambient / 温度: 298 K |
-NMR測定
NMRスペクトロメーター | タイプ: Varian INOVA / 製造業者: Varian / モデル: INOVA / 磁場強度: 600 MHz |
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-解析
NMR software |
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精密化 | 手法: simulated annealing / ソフトェア番号: 1 詳細: All structure calculations were carried out using the Ambiguous Restraints for Iterative Assignment of NOEs (ARIA) protocol Version 1.2, which includes an algorithm that attempts to correct ...詳細: All structure calculations were carried out using the Ambiguous Restraints for Iterative Assignment of NOEs (ARIA) protocol Version 1.2, which includes an algorithm that attempts to correct for the effects of spin diffusion, was use. Torsion Angle Likelihood Obtained from Shift and sequence similarity (TALOS) and was used to predict φ and ψ dihedral angle restraints. Initially, structure calculation runs contained 8 iterations of 20 structures each, with the best 7 structures in each iteration (sorted according to total energy) being used for analysis and assignment. The number of dynamics steps was increased over default values to 20000 and 16000 for the first and second cooling stages respectively. After each run, violated restraints were checked, and those arising from noise peaks or incorrect assignments were removed/reassigned. Final ensembles of 100 structures were calculated from calibrated restraint tables. The 20 best structures (sorted according to total energy) were selected for water refinement. Water refined structures were calculated using the slightly modified refinement script applied to the RECOORD database. PROCHECK and WHATCHECK and quality indicators were compared to the average values for the RECOORD database of protein NMR structures. | ||||||||||||||||
代表構造 | 選択基準: closest to the average | ||||||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: structures with the lowest energy 計算したコンフォーマーの数: 20 / 登録したコンフォーマーの数: 20 |