Database: EMDB / ID: EMD-32828
|Function / homology|
Function and homology information
enteropeptidase / scavenger receptor activity / brush border / serine-type endopeptidase activity / proteolysis / membrane
Similarity search - Function
Peptidase S1A, enteropeptidase / Scavenger receptor cysteine-rich domain / SRCR domain / SRCR domain profile. / Domain found in sea urchin sperm protein, enterokinase, agrin / SRCR-like domain / SRCR-like domain superfamily / Scavenger receptor Cys-rich / MAM domain signature. / SEA domain superfamily ...Peptidase S1A, enteropeptidase / Scavenger receptor cysteine-rich domain / SRCR domain / SRCR domain profile. / Domain found in sea urchin sperm protein, enterokinase, agrin / SRCR-like domain / SRCR-like domain superfamily / Scavenger receptor Cys-rich / MAM domain signature. / SEA domain superfamily / Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others) / SEA domain profile. / SEA domain / SEA domain / MAM domain, meprin/A5/mu / MAM domain / MAM domain profile. / CUB domain / Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein. / CUB domain / CUB domain profile. / Spermadhesin, CUB domain superfamily / Low-density lipoprotein (LDL) receptor class A, conserved site / LDL-receptor class A (LDLRA) domain signature. / Low-density lipoprotein receptor domain class A / LDL-receptor class A (LDLRA) domain profile. / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A repeat / LDL receptor-like superfamily / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain / Concanavalin A-like lectin/glucanase domain superfamily / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan
Similarity search - Domain/homology
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||single particle reconstruction / cryo EM / Resolution: 4.7 Å|
|Authors||Yang XL / Ding ZY / Huang HJ|
|Funding support||1 items |
|Citation||Journal: Nat Commun / Year: 2022|
Title: Cryo-EM structures reveal the activation and substrate recognition mechanism of human enteropeptidase.
Authors: Xiaoli Yang / Zhanyu Ding / Lisi Peng / Qiuyue Song / Deyu Zhang / Fang Cui / Chuanchao Xia / Keliang Li / Hua Yin / Shiyu Li / Zhaoshen Li / Haojie Huang /
Abstract: Enteropeptidase (EP) initiates intestinal digestion by proteolytically processing trypsinogen, generating catalytically active trypsin. EP dysfunction causes a series of pancreatic diseases including ...Enteropeptidase (EP) initiates intestinal digestion by proteolytically processing trypsinogen, generating catalytically active trypsin. EP dysfunction causes a series of pancreatic diseases including acute necrotizing pancreatitis. However, the molecular mechanisms of EP activation and substrate recognition remain elusive, due to the lack of structural information on the EP heavy chain. Here, we report cryo-EM structures of human EP in inactive, active, and substrate-bound states at resolutions from 2.7 to 4.9 Å. The EP heavy chain was observed to clamp the light chain with CUB2 domain for substrate recognition. The EP light chain N-terminus induced a rearrangement of surface-loops from inactive to active conformations, resulting in activated EP. The heavy chain then served as a hinge for light-chain conformational changes to recruit and subsequently cleave substrate. Our study provides structural insights into rearrangements of EP surface-loops and heavy chain dynamics in the EP catalytic cycle, advancing our understanding of EP-associated pancreatitis.
Downloads & links
|File||Download / File: emd_32828.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.046 Å|
|Symmetry||Space group: 1|
-Entire : Enteropeptidase
-Supramolecule #1: Enteropeptidase
|Supramolecule||Name: Enteropeptidase / type: complex / Chimera: Yes / ID: 1 / Parent: 0|
|Source (natural)||Organism: Homo sapiens (human)|
|Processing||single particle reconstruction|
|Vitrification||Cryogen name: ETHANE|
|Microscope||FEI TITAN KRIOS|
|Electron beam||Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN|
|Electron optics||Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3.4 µm / Nominal defocus min: 0.7000000000000001 µm|
|Image recording||Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 52.0 e/Å2|
Model: Titan Krios / Image courtesy: FEI Company
|Initial angle assignment||Type: PROJECTION MATCHING|
|Final angle assignment||Type: ANGULAR RECONSTITUTION|
|Final reconstruction||Resolution.type: BY AUTHOR / Resolution: 4.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 119676|
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