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Yorodumi- EMDB-40594: Xenopus laevis hyaluronan synthase 1, nascent HA polymer bound state -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-40594 | ||||||||||||
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Title | Xenopus laevis hyaluronan synthase 1, nascent HA polymer bound state | ||||||||||||
Map data | Xenopus laevis hyaluronan synthase 1, nascent HA polymer bound state | ||||||||||||
Sample |
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Keywords | hyaluronic acid / hyaluronan / HA / HAS / glycosyltransferase / GT / membrane protein / Fab / Transferase-Immune System complex | ||||||||||||
Function / homology | hyaluronan synthase / hyaluronan synthase activity / Glycosyltransferase like family 2 / extracellular matrix assembly / hyaluronan biosynthetic process / : / Nucleotide-diphospho-sugar transferases / membrane / Hyaluronan synthase 1 Function and homology information | ||||||||||||
Biological species | Xenopus laevis (African clawed frog) / Homo sapiens (human) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||||||||
Authors | Gorniak I / Zimmer J | ||||||||||||
Funding support | United States, Germany, 3 items
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Citation | Journal: To Be Published Title: Atomistic insights into hyaluronan synthesis, secretion, and length control Authors: Gorniak I / Stephens ZS / Erramilli SK / Gawda T / Kossiakoff AA / Zimmer J | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_40594.map.gz | 118 MB | EMDB map data format | |
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Header (meta data) | emd-40594-v30.xml emd-40594.xml | 22.3 KB 22.3 KB | Display Display | EMDB header |
Images | emd_40594.png | 32.7 KB | ||
Filedesc metadata | emd-40594.cif.gz | 6.9 KB | ||
Others | emd_40594_additional_1.map.gz emd_40594_half_map_1.map.gz emd_40594_half_map_2.map.gz | 117.6 MB 115.9 MB 115.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-40594 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-40594 | HTTPS FTP |
-Validation report
Summary document | emd_40594_validation.pdf.gz | 954.5 KB | Display | EMDB validaton report |
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Full document | emd_40594_full_validation.pdf.gz | 954 KB | Display | |
Data in XML | emd_40594_validation.xml.gz | 13.9 KB | Display | |
Data in CIF | emd_40594_validation.cif.gz | 16.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-40594 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-40594 | HTTPS FTP |
-Related structure data
Related structure data | 8smnMC 8smmC 8smpC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_40594.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Xenopus laevis hyaluronan synthase 1, nascent HA polymer bound state | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Additional Map
File | emd_40594_additional_1.map | ||||||||||||
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Annotation | Additional Map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half Map A
File | emd_40594_half_map_1.map | ||||||||||||
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Annotation | Half Map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half Map B
File | emd_40594_half_map_2.map | ||||||||||||
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Annotation | Half Map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Xenopus laevis hyaluronan synthase 1 in complex with a Fab molecu...
Entire | Name: Xenopus laevis hyaluronan synthase 1 in complex with a Fab molecule, nascent HA polymer bound state |
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Components |
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-Supramolecule #1: Xenopus laevis hyaluronan synthase 1 in complex with a Fab molecu...
Supramolecule | Name: Xenopus laevis hyaluronan synthase 1 in complex with a Fab molecule, nascent HA polymer bound state type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: Xenopus laevis (African clawed frog) |
Molecular weight | Theoretical: 118 KDa |
-Macromolecule #1: Hyaluronan synthase 1
Macromolecule | Name: Hyaluronan synthase 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: hyaluronan synthase |
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Source (natural) | Organism: Xenopus laevis (African clawed frog) |
Molecular weight | Theoretical: 70.385047 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MHHHHHHHHH HHHMKEKAAE TMEIPEGIPK DLEPKHPTLW RIIYYSFGVV LLATITAAYV AEFQVLKHEA ILFSLGLYGL AMLLHLMMQ SLFAFLEIRR VNKSELPCSF KKTVALTIAG YQENPEYLIK CLESCKYVKY PKDKLKIILV IDGNTEDDAY M MEMFKDVF ...String: MHHHHHHHHH HHHMKEKAAE TMEIPEGIPK DLEPKHPTLW RIIYYSFGVV LLATITAAYV AEFQVLKHEA ILFSLGLYGL AMLLHLMMQ SLFAFLEIRR VNKSELPCSF KKTVALTIAG YQENPEYLIK CLESCKYVKY PKDKLKIILV IDGNTEDDAY M MEMFKDVF HGEDVGTYVW KGNYHTVKKP EETNKGSCPE VSKPLNEDEG INMVEELVRN KRCVCIMQQW GGKREVMYTA FQ AIGTSVD YVQVCDSDTK LDELATVEMV KVLESNDMYG AVGGDVRILN PYDSFISFMS SLRYWMAFNV ERACQSYFDC VSC ISGPLG MYRNNILQVF LEAWYRQKFL GTYCTLGDDR HLTNRVLSMG YRTKYTHKSR AFSETPSLYL RWLNQQTRWT KSYF REWLY NAQWWHKHHI WMTYESVVSF IFPFFITATV IRLIYAGTIW NVVWLLLCIQ IMSLFKSIYA CWLRGNFIML LMSLY SMLY MTGLLPSKYF ALLTLNKTGW GTSGRKKIVG NYMPILPLSI WAAVLCGGVG YSIYMDCQND WSTPEKQKEM YHLLYG CVG YVMYWVIMAV MYWVWVKRCC RKRSQTVTLV HDIPDMCV UniProtKB: Hyaluronan synthase 1 |
-Macromolecule #2: Fab15 heavy chain
Macromolecule | Name: Fab15 heavy chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 24.674379 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: EISEVQLVES GGGLVQPGGS LRLSCAASGF NVSSYYIHWV RQAPGKGLEW VASISSSSGS TSYADSVKGR FTISADTSKN TAYLQMNSL RAEDTAVYYC ARSGYYWGPY FGGFDYWGQG TLVTVSSAST KGPSVFPLAP SSKSTSGGTA ALGCLVKDYF P EPVTVSWN ...String: EISEVQLVES GGGLVQPGGS LRLSCAASGF NVSSYYIHWV RQAPGKGLEW VASISSSSGS TSYADSVKGR FTISADTSKN TAYLQMNSL RAEDTAVYYC ARSGYYWGPY FGGFDYWGQG TLVTVSSAST KGPSVFPLAP SSKSTSGGTA ALGCLVKDYF P EPVTVSWN SGALTSGVHT FPAVLQSSGL YSLSSVVTVP SSSLGTQTYI CNVNHKPSNT KVDKKVEPKS CDKTHT |
-Macromolecule #3: Fab15 light chain
Macromolecule | Name: Fab15 light chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 23.258783 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: SDIQMTQSPS SLSASVGDRV TITCRASQSV SSAVAWYQQK PGKAPKLLIY SASSLYSGVP SRFSGSRSGT DFTLTISSLQ PEDFATYYC QQSSSSLITF GQGTKVEIKR TVAAPSVFIF PPSDSQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN S QESVTEQD ...String: SDIQMTQSPS SLSASVGDRV TITCRASQSV SSAVAWYQQK PGKAPKLLIY SASSLYSGVP SRFSGSRSGT DFTLTISSLQ PEDFATYYC QQSSSSLITF GQGTKVEIKR TVAAPSVFIF PPSDSQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN S QESVTEQD SKDSTYSLSS TLTLSKADYE KHKVYACEVT HQGLSSPVTK SFNRGEC |
-Macromolecule #5: water
Macromolecule | Name: water / type: ligand / ID: 5 / Number of copies: 1 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 8 mg/mL | ||||||||||||
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Buffer | pH: 7.8 Component:
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Grid | Model: C-flat-1.2/1.3 / Support film - Material: CARBON / Support film - topology: HOLEY | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 20.0 µm / Nominal defocus min: 10.0 µm / Nominal magnification: 81000 |
Sample stage | Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Protocol: RIGID BODY FIT |
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Output model | PDB-8smn: |