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基本情報
登録情報 | データベース: PDB / ID: 2btf | ||||||
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タイトル | THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN | ||||||
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![]() | ACETYLATION AND ACTIN-BINDING | ||||||
機能・相同性 | ![]() PCP/CE pathway / Adherens junctions interactions / Cell-extracellular matrix interactions / B-WICH complex positively regulates rRNA expression / Gap junction degradation / Formation of annular gap junctions / MAP2K and MAPK activation / RHOF GTPase cycle / EPHB-mediated forward signaling / Regulation of actin dynamics for phagocytic cup formation ...PCP/CE pathway / Adherens junctions interactions / Cell-extracellular matrix interactions / B-WICH complex positively regulates rRNA expression / Gap junction degradation / Formation of annular gap junctions / MAP2K and MAPK activation / RHOF GTPase cycle / EPHB-mediated forward signaling / Regulation of actin dynamics for phagocytic cup formation / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / DNA Damage Recognition in GG-NER / UCH proteinases / VEGFA-VEGFR2 Pathway / structural constituent of postsynaptic actin cytoskeleton / positive regulation of actin filament bundle assembly / dense body / regulation of actin filament polymerization / Clathrin-mediated endocytosis / NuA4 histone acetyltransferase complex / axonogenesis / cell motility / actin filament / 加水分解酵素; 酸無水物に作用; 酸無水物に作用・細胞または細胞小器官の運動に関与 / actin cytoskeleton / actin binding / actin cytoskeleton organization / cytoskeleton / hydrolase activity / axon / focal adhesion / synapse / protein kinase binding / protein-containing complex / ATP binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | ![]() | ||||||
![]() | Schutt, C.E. / Myslik, J.C. / Rozycki, M.D. / Goonesekere, N.C.W. | ||||||
![]() | ![]() タイトル: The structure of crystalline profilin-beta-actin. 著者: Schutt, C.E. / Myslik, J.C. / Rozycki, M.D. / Goonesekere, N.C. / Lindberg, U. #1: ![]() タイトル: Structural Aspects of Actin Binding Proteins Current Opinion in Cell Biology 著者: Rozycki, M.D. / Myslik, J.C. / Schutt, C.E. / Lindberg, U. #2: ![]() タイトル: Mutagenesis of Human Profilin Locates its Poly(L-Proline)-Binding Site to a Hydrophobic Patch of Aromatic Amino Acids 著者: Bjorkegren, C. / Rozycki, M. / Schutt, C.E. / Lindberg, U. / Karlsson, R. #3: ![]() タイトル: Molecular Packing in Profilin-Actin Crystals and its Implications 著者: Schutt, C.E. / Lindberg, U. / Myslik, J. / Strauss, N. | ||||||
履歴 |
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Remark 650 | HELIX RESIDUES ARE INCLUDED AT THE BEGINNING OF HELICES IF THEY PARTICIPATE IN HYDROGEN BONDING AND ...HELIX RESIDUES ARE INCLUDED AT THE BEGINNING OF HELICES IF THEY PARTICIPATE IN HYDROGEN BONDING AND ARE "PARTIALLY" HELICAL, EVEN IF THE ENTIRE RESIDUE DOES NOT FIT HELICAL CRITERIA. | ||||||
Remark 700 | SHEET PROFILIN IS DESCRIBED IN JRNL REFERENCE AS HAVING A SIX-MEMBERED BETA-SHEET WHICH SHARES A ...SHEET PROFILIN IS DESCRIBED IN JRNL REFERENCE AS HAVING A SIX-MEMBERED BETA-SHEET WHICH SHARES A STRAND WITH A SECOND TWO-MEMBERED SHEET. TO CONFORM WITH PROTEIN DATA BANK GUIDELINES, THESE SHEETS ARE COMBINED INTO A SINGLE SEVEN-MEMBERED SHEET (SP1) IN THIS ENTRY. STRAND NUMBERING ALSO DIFFERS FROM THE JRNL REFERENCE. SECONDARY STRUCTURE ASSIGNMENTS FOR BETA-ACTIN ARE SIMILAR TO THOSE USED FOR ALPHA-ACTIN (PROTEIN DATA BANK ENTRY 1ATN) WITH MINOR CHANGES. HOWEVER, THE NOMENCLATURE USED HEREIN DIFFERS FROM THAT USED IN THE ABOVE ENTRY. ALSO, STRAND A4B DESCRIBED IN THAT ENTRY IS NOT INCLUDED HERE BECAUSE THE "ALTERNATIVE" STRAND TO ONE IN STRAND A4A (CORRESPONDING TO SA4 IN THIS ENTRY) IS ONLY TWO RESIDUES IN LENGTH. IN CONTRAST, SHEET SA3 IS INCLUDED BECAUSE IT CONTAINS TWO STRANDS AND A WELL-DEFINED TYPE II TURN, EVEN THOUGH THE TWO STRANDS CONTAIN ONLY TWO RESIDUES EACH. RESIDUE P 31 IS A BETA-BULGE. RESIDUE P 73 IS A BETA-BULGE, REDIRECTING STRAND 6. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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-検証レポート
文書・要旨 | ![]() | 474 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 498.8 KB | 表示 | |
XML形式データ | ![]() | 15.1 KB | 表示 | |
CIF形式データ | ![]() | 21.4 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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単位格子 |
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Atom site foot note | 1: RESIDUE ACE A IS THE N-ACETYL MOIETY OF ACTIN. / 2: RESIDUE A 73 IS 3-METHYL HISTIDYL. / 3: RESIDUE ACE P IS THE N-ACETYL MOIETY OF PROFILIN. / 4: RESIDUE P 31 IS A BETA-BULGE. / 5: RESIDUE P 73 IS A BETA-BULGE, REDIRECTING STRAND 6. |
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要素
#1: タンパク質 | 分子量: 41690.520 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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#2: タンパク質 | 分子量: 14968.185 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
#3: 化合物 | ChemComp-SR / |
#4: 化合物 | ChemComp-ATP / |
-実験情報
-実験
実験 | 手法: ![]() |
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試料調製
結晶 | マシュー密度: 2.11 Å3/Da / 溶媒含有率: 41.6 % | ||||||||||||||||||||||||||||||
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結晶化 | *PLUS 温度: 4 ℃ / 手法: 蒸気拡散法, ハンギングドロップ法詳細: referred to 'Segura, M. & Lindberg, U.', (1984) J.Biol.Chem., 259, 3949-3954 | ||||||||||||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
放射 | 散乱光タイプ: x-ray |
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放射波長 | 相対比: 1 |
反射 | *PLUS 最高解像度: 2.55 Å / Num. obs: 16158 / % possible obs: 98.8 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.065 |
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解析
ソフトウェア |
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精密化 | Rfactor Rwork: 0.199 / Rfactor obs: 0.199 / 最高解像度: 2.55 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 2.55 Å
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拘束条件 |
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精密化 | *PLUS 最低解像度: 8 Å / σ(F): 3 / Rfactor obs: 0.199 / Rfactor Rwork: 0.199 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
溶媒の処理 | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | *PLUS Biso mean: 19.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
拘束条件 | *PLUS タイプ: x_angle_d / Dev ideal: 3.8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS精密化 シェル | *PLUS 最高解像度: 2.55 Å / 最低解像度: 2.66 Å / Total num. of bins used: 8 / Num. reflection obs: 1539 / Rfactor obs: 0.2961 |