+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-11658 | |||||||||
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Title | MUC2 amino terminal D1D2D3CysD1 2 bead map | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
Authors | Javitt G / Fass D | |||||||||
Citation | Journal: Cell / Year: 2020 Title: Assembly Mechanism of Mucin and von Willebrand Factor Polymers. Authors: Gabriel Javitt / Lev Khmelnitsky / Lis Albert / Lavi Shlomo Bigman / Nadav Elad / David Morgenstern / Tal Ilani / Yaakov Levy / Ron Diskin / Deborah Fass / Abstract: The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food. Likewise, the vasculature is threatened by inflammation and trauma. Mucin ...The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food. Likewise, the vasculature is threatened by inflammation and trauma. Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems. Colon mucins additionally house and feed the gut microbiome. Here, we present an integrated structural analysis of the intestinal mucin MUC2. Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels. Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus. Remarkably, a densely O-glycosylated mucin domain performs an organizational role in MUC2. The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_11658.map.gz | 238.9 MB | EMDB map data format | |
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Header (meta data) | emd-11658-v30.xml emd-11658.xml | 13.8 KB 13.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_11658_fsc.xml | 22.9 KB | Display | FSC data file |
Images | emd_11658.png | 108.2 KB | ||
Others | emd_11658_half_map_1.map.gz emd_11658_half_map_2.map.gz | 443 MB 443 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11658 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11658 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_11658.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 0.859 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: #1
File | emd_11658_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_11658_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Filament of amino terminal MUC2 comprised of domains D1D2D3CysD1
Entire | Name: Filament of amino terminal MUC2 comprised of domains D1D2D3CysD1 |
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Components |
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-Supramolecule #1: Filament of amino terminal MUC2 comprised of domains D1D2D3CysD1
Supramolecule | Name: Filament of amino terminal MUC2 comprised of domains D1D2D3CysD1 type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Homo sapiens (human) |
-Macromolecule #1: MUC2 D1D2D3CysD1
Macromolecule | Name: MUC2 D1D2D3CysD1 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: SELQTEGRTR YHGRNVCSTW GNFHYKTFDG DVFRFPGLCD YNFASDCRGS YKEFAVHLKR GPGQAEAPAG VESILLTIKD DTIYLTRHLA VLNGAVVSTP HYSPGLLIE KSDAYTKVYS RAGLTLMWNR EDALMLELDT KFRNHTCGLC GDYNGLQSYS EFLSDGVLFS ...String: SELQTEGRTR YHGRNVCSTW GNFHYKTFDG DVFRFPGLCD YNFASDCRGS YKEFAVHLKR GPGQAEAPAG VESILLTIKD DTIYLTRHLA VLNGAVVSTP HYSPGLLIE KSDAYTKVYS RAGLTLMWNR EDALMLELDT KFRNHTCGLC GDYNGLQSYS EFLSDGVLFS PLEFGNMQKI NQPDVVCEDP EEEVAPASCS E HRAECERL LTAEAFADCQ DLVPLEPYLR ACQQDRCRCP GGDTCVCSTV AEFSRQCSHA GGRPGNWRTA TLCPKTCPGN LVYLESGSPC MDTCSHLEVS SL CEEHRMD GCFCPEGTVY DDIGDSGCVP VSQCHCRLHG HLYTPGQEIT NDCEQCVCNA GRWVCKDLPC PGTCALEGGS HITTFDGKTY TFHGDCYYVL AKG DHNDSY ALLGELAPCG STDKQTCLKT VVLLADKKKN AVVFKSDGSV LLNQLQVNLP HVTASFSVFR PSSYHIMVSM AIGVRLQVQL APVMQLFVTL DQAS QGQVQ GLCGNFNGLE GDDFKTASGL VEATGAGFAN TWKAQSTCHD KLDWLDDPCS LNIESANYAE HWCSLLKKTE TPFGRCHSAV DPAEYYKRCK YDTCN CQNN EDCLCAALSS YARACTAKGV MLWGWREHVC NKDVGSCPNS QVFLYNLTTC QQTCRSLSEA DSHCLEGFAP VDGCGCPDHT FLDEKGRCVP LAKCSC YHR GLYLEAGDVV VRQEERCVCR DGRLHCRQIR LIGQSCTAPK IHMDCSNLTA LATSKPRALS CQTLAAGYYH TECVSGCVCP DGLMDDGRGG CVVEKEC PC VHNNDLYSSG AKIKVDCNTC TCKRGRWVCT QAVCHGTCSI YGSGHYITFD GKYYDFDGHC SYVAVQDYCG QNSSLGSFSI ITENVPCGTT GVTCSKAI K IFMGRTELKL EDKHRVVIQR DEGHHVAYTT REVGQYLVVE SSTGIIVIWD KRTTVFIKLA PSYKGTVCGL CGNFDHRSNN DFTTRDHMVV SSELDFGNS WKEAPTCPDV STNPEPCSLN PHRRSWAEKQ CSILKSSVFS ICHSKVDPKP FYEACVHDSC SCDTGGDCEC FCSAVASYAQ ECTKEGACVF WRTPDLCPIF CDYYNPPHE CEWHYEPCGN RSFETCRTIN GIHSNISVSY LEGCYPRCPK DRPIYEEDLK KCVTADKCGC YVEDTHYPPG ASVPTEETCK SCVCTNSSQV V CRPEEGKI LNQTQDGAFC YWEICGPNGT VEKHFNICSI TTRPSTLTTF TTITLPTTPT SFTTTTTTTT PTSSTVLSTT PKLCCLWSDW INEDHPSSGS DD GDRETFD GVCGAPEDIE CRSVKDPHLS LEQHGQKVQC DVSVGFICKN EDQFGNGPFG LCYDYKIRVN CCWPMDKCIT HHHHHH |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | filament |
-Sample preparation
Buffer | pH: 5.7 |
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Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 30.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |