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Open data
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Basic information
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Title | Cryo-EM structure of human hyaluronidase PH-20 | |||||||||
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![]() | hyaluronidase / endoglycosidase hydrolase / fab complex / HYDROLASE / HYDROLASE-IMMUNE SYSTEM complex | |||||||||
Function / homology | ![]() hyaluronoglucosaminidase / Interaction With Cumulus Cells And The Zona Pellucida / fusion of sperm to egg plasma membrane involved in single fertilization / hyalurononglucosaminidase activity / hyaluronan catabolic process / binding of sperm to zona pellucida / side of membrane / acrosomal vesicle / carbohydrate metabolic process / cell adhesion / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
![]() | Im S-B / Jeong T-K / Kim N / Oh B-H | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM Structure of Human Hyaluronidase PH-20. Authors: Seong-Bin Im / Hyung Nam Song / Tae-Kyeong Jeong / Nayun Kim / Kyuwan Kim / Soon-Jae Park / Byung-Ha Oh / ![]() Abstract: PH-20 is a specific type of hyaluronidase that plays a critical role in the fertilization process by facilitating the initial binding of sperm to the glycoprotein layer surrounding the oocyte and ...PH-20 is a specific type of hyaluronidase that plays a critical role in the fertilization process by facilitating the initial binding of sperm to the glycoprotein layer surrounding the oocyte and subsequently breaking down hyaluronic acid polymers in the cumulus cell layer. PH-20 contains an epidermal growth factor (EGF)-like domain, which may be involved in the recognition of the glycoprotein layer in addition to the catalytic domain. Herein, we report the structure of human PH-20 determined by cryogenic electron microscopy. Comparative analyses of the PH-20 structure with two other available hyaluronidase structures reveal a general similarity in the central catalytic domains, including the conservation of catalytically essential residues at the equivalent spatial positions. However, unique difference is found in the EGF-like domain, characterized by a longer sequence that is likely to form a flexibly anchored β-hairpin containing a disulfide bond. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 229.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.6 KB 20.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.2 KB | Display | ![]() |
Images | ![]() | 70.1 KB | ||
Filedesc metadata | ![]() | 6.4 KB | ||
Others | ![]() ![]() | 226.4 MB 226.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9jubMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.664 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_61826_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_61826_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Complex of human hyaluronidase PH-20 and 79C11Fab
Entire | Name: Complex of human hyaluronidase PH-20 and 79C11Fab |
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Components |
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-Supramolecule #1: Complex of human hyaluronidase PH-20 and 79C11Fab
Supramolecule | Name: Complex of human hyaluronidase PH-20 and 79C11Fab / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Molecular weight | Theoretical: 90 KDa |
-Supramolecule #2: hyaluronidase PH-20
Supramolecule | Name: hyaluronidase PH-20 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
-Supramolecule #3: 79C11Fab
Supramolecule | Name: 79C11Fab / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Hyaluronidase PH-20
Macromolecule | Name: Hyaluronidase PH-20 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: hyaluronoglucosaminidase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 46.610211 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: NFRAPPVIPN VPFLWAWNAP SEFCLGKFDE PLDMSLFSFI GSPRINATGQ GVTIFYVDRL GYYPYIDSIT GVTVNGGIPQ KISLQDHLD KAKKDITFYM PVDNLGMAVI DWEEWRPTWA RNWKPKDVYK NRSIELVQQQ NVQLSLTEAT EKAKQEFEKA G KDFLVETI ...String: NFRAPPVIPN VPFLWAWNAP SEFCLGKFDE PLDMSLFSFI GSPRINATGQ GVTIFYVDRL GYYPYIDSIT GVTVNGGIPQ KISLQDHLD KAKKDITFYM PVDNLGMAVI DWEEWRPTWA RNWKPKDVYK NRSIELVQQQ NVQLSLTEAT EKAKQEFEKA G KDFLVETI KLGKLLRPNH LWGYYLFPDC YNHHYKKPGY NGSCFNVEIK RNDDLSWLWN ESTALYPSIY LNTQQSPVAA TL YVRNRVR EAIRVSKIPD AKSPLPVFAY TRIVFTDQVL KFLSQDELVY TFGETVALGA SGIVIWGTLS IMRSMKSCLL LDN YMETIL NPYIINVTLA AKMCSQVLCQ EQGVCIRKNW NSSDYLHLNP DNFAIQLEKG GKFTVRGKPT LEDLEQFSEK FYCS CYSTL S UniProtKB: Hyaluronidase PH-20 |
-Macromolecule #2: Heavy chain of 79C11Fab
Macromolecule | Name: Heavy chain of 79C11Fab / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 22.664252 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: QSVEESGGRL VTPGGSLTLT CTVSGFSLSS NAISWVRQAP GKGLEYIGII STSGSTYYAN WAKGRFTISK TSTTVDLKMT SLTTEDTAT YFCARDGAYD DFAYYFDLWG QGTLVTVSSG QPKAPSVFPL APCCGDTPSS TVTLGCLVKG YLPEPVTVTW N SGTLTNGV ...String: QSVEESGGRL VTPGGSLTLT CTVSGFSLSS NAISWVRQAP GKGLEYIGII STSGSTYYAN WAKGRFTISK TSTTVDLKMT SLTTEDTAT YFCARDGAYD DFAYYFDLWG QGTLVTVSSG QPKAPSVFPL APCCGDTPSS TVTLGCLVKG YLPEPVTVTW N SGTLTNGV RTFPSVRQSS GLYSLSSVVS VTSSSQPVTC NVAHPATNTK VDKTVAPS |
-Macromolecule #3: Light chain of 79C11Fab
Macromolecule | Name: Light chain of 79C11Fab / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 22.270688 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: ALVMTQTPSS VSAAVGGTVT INCQASQNIY SGLAWYQQKL GQPPKLLIYK ASTLASGVPS RFKGSGSGTQ FTLTISGVQC DDAATYYCQ LAYSSTNVDN AFGGGTEVVV KGDPVAPTVL IFPPAADQVA TGTVTIVCVA NKYFPDVTVT WEVDGTTQTT G IENSKTPQ ...String: ALVMTQTPSS VSAAVGGTVT INCQASQNIY SGLAWYQQKL GQPPKLLIYK ASTLASGVPS RFKGSGSGTQ FTLTISGVQC DDAATYYCQ LAYSSTNVDN AFGGGTEVVV KGDPVAPTVL IFPPAADQVA TGTVTIVCVA NKYFPDVTVT WEVDGTTQTT G IENSKTPQ NSADCTYNLS STLTLTSTQY NSHKEYTCKV TQGTTSVVQS FNRG |
-Macromolecule #5: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 5 / Number of copies: 3 / Formula: NAG |
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Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 69.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.3000000000000003 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |