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基本情報
登録情報 | データベース: EMDB / ID: EMD-12887 | |||||||||
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タイトル | Folded elbow of cohesin | |||||||||
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![]() | Cohesin / Elbow / Hinge / Smc1 / Smc3 / coiled coil / DNA / CELL CYCLE | |||||||||
機能・相同性 | ![]() Establishment of Sister Chromatid Cohesion / Resolution of Sister Chromatid Cohesion / meiotic cohesin complex / establishment of meiotic sister chromatid cohesion / cohesin complex / DNA secondary structure binding / mitotic cohesin complex / SUMOylation of DNA damage response and repair proteins / synaptonemal complex assembly / meiotic sister chromatid cohesion ...Establishment of Sister Chromatid Cohesion / Resolution of Sister Chromatid Cohesion / meiotic cohesin complex / establishment of meiotic sister chromatid cohesion / cohesin complex / DNA secondary structure binding / mitotic cohesin complex / SUMOylation of DNA damage response and repair proteins / synaptonemal complex assembly / meiotic sister chromatid cohesion / replication-born double-strand break repair via sister chromatid exchange / establishment of mitotic sister chromatid cohesion / reciprocal meiotic recombination / sister chromatid cohesion / mitotic sister chromatid cohesion / mitotic sister chromatid segregation / minor groove of adenine-thymine-rich DNA binding / G2/M transition of mitotic cell cycle / double-strand break repair / double-stranded DNA binding / cell division / protein kinase binding / ATP hydrolysis activity / DNA binding / ATP binding / identical protein binding / nucleus 類似検索 - 分子機能 | |||||||||
生物種 | ![]() ![]() ![]() ![]() | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 5.5 Å | |||||||||
![]() | Gonzalez Llamazares A / Lee B-G / Collier J / Nasmyth KA / Lowe J | |||||||||
![]() | ![]() タイトル: Folding of cohesin's coiled coil is important for Scc2/4-induced association with chromosomes. 著者: Naomi J Petela / Andres Gonzalez Llamazares / Sarah Dixon / Bin Hu / Byung-Gil Lee / Jean Metson / Heekyo Seo / Antonio Ferrer-Harding / Menelaos Voulgaris / Thomas Gligoris / James Collier / ...著者: Naomi J Petela / Andres Gonzalez Llamazares / Sarah Dixon / Bin Hu / Byung-Gil Lee / Jean Metson / Heekyo Seo / Antonio Ferrer-Harding / Menelaos Voulgaris / Thomas Gligoris / James Collier / Byung-Ha Oh / Jan Löwe / Kim A Nasmyth / ![]() ![]() 要旨: Cohesin's association with and translocation along chromosomal DNAs depend on an ATP hydrolysis cycle driving the association and subsequent release of DNA. This involves DNA being 'clamped' by Scc2 ...Cohesin's association with and translocation along chromosomal DNAs depend on an ATP hydrolysis cycle driving the association and subsequent release of DNA. This involves DNA being 'clamped' by Scc2 and ATP-dependent engagement of cohesin's Smc1 and Smc3 head domains. Scc2's replacement by Pds5 abrogates cohesin's ATPase and has an important role in halting DNA loop extrusion. The ATPase domains of all SMC proteins are separated from their hinge dimerisation domains by 50-nm-long coiled coils, which have been observed to zip up along their entire length and fold around an elbow, thereby greatly shortening the distance between hinges and ATPase heads. Whether folding exists in vivo or has any physiological importance is not known. We present here a cryo-EM structure of the form of cohesin that reveals the structure of folded and zipped-up coils in unprecedented detail and shows that Scc2 can associate with Smc1's ATPase head even when it is fully disengaged from that of Smc3. Using cysteine-specific crosslinking, we show that cohesin's coiled coils are frequently folded in vivo, including when cohesin holds sister chromatids together. Moreover, we describe a mutation () within Smc1's hinge that alters how Scc2 and Pds5 interact with Smc1's hinge and that enables Scc2 to support loading in the absence of its normal partner Scc4. The mutant phenotype of loading without Scc4 is only explicable if loading depends on an association between Scc2/4 and cohesin's hinge, which in turn requires coiled coil folding. | |||||||||
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構造の表示
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構造ビューア | EMマップ: ![]() ![]() ![]() |
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マップデータ | ![]() | 2.1 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 13.3 KB 13.3 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 7.2 KB | 表示 | ![]() |
画像 | ![]() | 23.7 KB | ||
Filedesc metadata | ![]() | 6.8 KB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 346.7 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 346.3 KB | 表示 | |
XML形式データ | ![]() | 9.6 KB | 表示 | |
CIF形式データ | ![]() | 12.5 KB | 表示 | |
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マップ
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ボクセルのサイズ | X=Y=Z: 1.96 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
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試料の構成要素
-全体 : Cohesin
全体 | 名称: Cohesin |
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要素 |
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-超分子 #1: Cohesin
超分子 | 名称: Cohesin / タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: all |
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由来(天然) | 生物種: ![]() ![]() |
-分子 #1: Structural maintenance of chromosomes protein 1
分子 | 名称: Structural maintenance of chromosomes protein 1 / タイプ: protein_or_peptide / ID: 1 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() ![]() 株: ATCC 204508 / S288c |
分子量 | 理論値: 141.491781 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MGRLVGLELS NFKSYRGVTK VGFGESNFTS IIGPNGSGKS NMMDAISFVL GVRSNHLRSN ILKDLIYRGV LNDENSDDYD NEGAASSNP QSAYVKAFYQ KGNKLVELMR IISRNGDTSY KIDGKTVSYK DYSIFLENEN ILIKAKNFLV FQGDVEQIAA Q SPVELSRM ...文字列: MGRLVGLELS NFKSYRGVTK VGFGESNFTS IIGPNGSGKS NMMDAISFVL GVRSNHLRSN ILKDLIYRGV LNDENSDDYD NEGAASSNP QSAYVKAFYQ KGNKLVELMR IISRNGDTSY KIDGKTVSYK DYSIFLENEN ILIKAKNFLV FQGDVEQIAA Q SPVELSRM FEEVSGSIQY KKEYEELKEK IEKLSKSATE SIKNRRRIHG ELKTYKEGIN KNEEYRKQLD KKNELQKFQA LW QLYHLEQ QKEELTDKLS ALNSEISSLK GKINNEMKSL QRSKSSFVKE SAVISKQKSK LDYIFKDKEK LVSDLRLIKV PQQ AAGKRI SHIEKRIESL QKDLQRQKTY VERFETQLKV VTRSKEAFEE EIKQSARNYD KFKLNENDLK TYNCLHEKYL TEGG SILEE KIAVLNNDKR EIQEELERFN KRADISKRRI TEELSITGEK LDTQLNDLRV SLNEKNALHT ERLHELKKLQ SDIES ANNQ EYDLNFKLRE TLVKIDDLSA NQRETMKERK LRENIAMLKR FFPGVKGLVH DLCHPKKEKY GLAVSTILGK NFDSVI VEN LTVAQECIAF LKKQRAGTAS FIPLDTIETE LPTLSLPDSQ DYILSINAID YEPEYEKAMQ YVCGDSIICN TLNIAKD LK WKKGIRGKLV TIEGALIHKA GLMTGGISGD ANNRWDKEEY QSLMSLKDKL LIQIDELSNG QRSNSIRARE VENSVSLL N SDIANLRTQV TQQKRSLDEN RLEIKYHNDL IEKEIQPKIT ELKKKLDDLE NTKDNLVKEK EALQNNIFKE FTSKIGFTI KEYENHSGEL MRQQSKELQQ LQKQILTVEN KLQFETDRLS TTQRRYEKAQ KDLENAQVEM KSLEEQEYAI EMKIGSIESK LEEHKNHLD ELQKKFVTKQ SELNSSEDIL EDMNSNLQVL KRERDGIKED IEKFDLERVT ALKNCKISNI NIPISSETTI D DLPISSTD NEAITISNSI DINYKGLPKK YKENNTDSAR KELEQKIHEV EEILNELQPN ARALERYDEA EGRFEVINNE TE QLKAEEK KILNQFLKIK KKRKELFEKT FDYVSDHLDA IYRELTKNPN SNVELAGGNA SLTIEDEDEP FNAGIKYHAT PPL KRFKDM EYLSGGEKTV AALALLFAIN SYQPSPFFVL DEVDAALDIT NVQRIAAYIR RHRNPDLQFI VISLKNTMFE KSDA LVGVY RQQQENSSKI ITLDLSNYAE UniProtKB: Structural maintenance of chromosomes protein 1 |
-分子 #2: Structural maintenance of chromosomes protein 3
分子 | 名称: Structural maintenance of chromosomes protein 3 / タイプ: protein_or_peptide / ID: 2 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() ![]() 株: ATCC 204508 / S288c |
分子量 | 理論値: 141.539984 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MYIKRVIIKG FKTYRNETII DNFSPHQNVI IGSNGSGKSN FFAAIRFVLS DDYSNLKREE RQGLIHQGSG GSVMSASVEI VFHDPDHSM ILPSGVLSRG DDEVTIRRTV GLKKDDYQLN DRNVTKGDIV RMLETAGFSM NNPYNIVPQG KIVALTNAKD K ERLQLLED ...文字列: MYIKRVIIKG FKTYRNETII DNFSPHQNVI IGSNGSGKSN FFAAIRFVLS DDYSNLKREE RQGLIHQGSG GSVMSASVEI VFHDPDHSM ILPSGVLSRG DDEVTIRRTV GLKKDDYQLN DRNVTKGDIV RMLETAGFSM NNPYNIVPQG KIVALTNAKD K ERLQLLED VVGAKSFEVK LKASLKKMEE TEQKKIQINK EMGELNSKLS EMEQERKELE KYNELERNRK IYQFTLYDRE LN EVINQME RLDGDYNNTV YSSEQYIQEL DKREDMIDQV SKKLSSIEAS LKIKNATDLQ QAKLRESEIS QKLTNVNVKI KDV QQQIES NEEQRNLDSA TLKEIKSIIE QRKQKLSKIL PRYQELTKEE AMYKLQLASL QQKQRDLILK KGEYARFKSK DERD TWIHS EIEELKSSIQ NLNELESQLQ MDRTSLRKQY SAIDEEIEEL IDSINGPDTK GQLEDFDSEL IHLKQKLSES LDTRK ELWR KEQKLQTVLE TLLSDVNQNQ RNVNETMSRS LANGIINVKE ITEKLKISPE SVFGTLGELI KVNDKYKTCA EVIGGN SLF HIVVDTEETA TLIMNELYRM KGGRVTFIPL NRLSLDSDVK FPSNTTTQIQ FTPLIKKIKY EPRFEKAVKH VFGKTIV VK DLGQGLKLAK KHKLNAITLD GDRADKRGVL TGGYLDQHKR TRLESLKNLN ESRSQHKKIL EELDFVRNEL NDIDTKID Q VNGNIRKVSN DRESVLTNIE VYRTSLNTKK NEKLILEESL NAIILKLEKL NTNRTFAQEK LNTFENDLLQ EFDSELSKE EKERLESLTK EISAAHNKLN ITSDALEGIT TTIDSLNAEL ESKLIPQEND LESKMSEVGD AFIFGLQDEL KELQLEKESV EKQHENAVL ELGTVQREIE SLIAEETNNK KLLEKANNQQ RLLLKKLDNF QKSVEKTMIK KTTLVTRREE LQQRIREIGL L PEDALVND FSDITSDQLL QRLNDMNTEI SGLKNVNKRA FENFKKFNER RKDLAERASE LDESKDSIQD LIVKLKQQKV NA VDSTFQK VSENFEAVFE RLVPRGTAKL IIHRKNDNAN DHDESIDVDM DAESNESQNG KDSEIMYTGV SISVSFNSKQ NEQ LHVEQL SGGQKTVCAI ALILAIQMVD PASFYLFDEI DAALDKQYRT AVATLLKELS KNAQFICTTF RTDMLQVADK FFRV KYENK ISTVIEVNRE EAIGFIRGSN KFAEV UniProtKB: Structural maintenance of chromosomes protein 3 |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.5 |
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グリッド | モデル: Quantifoil R2/2 / 材質: COPPER/RHODIUM / メッシュ: 200 / 前処理 - タイプ: GLOW DISCHARGE / 前処理 - 時間: 45 sec. |
凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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特殊光学系 | 位相板: VOLTA PHASE PLATE / エネルギーフィルター - スリット幅: 20 eV |
撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 検出モード: COUNTING / 平均電子線量: 42.5 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm |
試料ステージ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |