Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural and functional insights into Escherichia coli α2-macroglobulin endopeptidase snap-trap inhibition.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 112, Issue 27, Page 8290-8295, Year 2015
Publish date	Jul 7, 2015
Authors	Irene Garcia-Ferrer / Pedro Arêde / Josué Gómez-Blanco / Daniel Luque / Stephane Duquerroy / José R Castón / Theodoros Goulas / F Xavier Gomis-Rüth /
PubMed Abstract	The survival of commensal bacteria requires them to evade host peptidases. Gram-negative bacteria from the human gut microbiome encode a relative of the human endopeptidase inhibitor, α2- ...The survival of commensal bacteria requires them to evade host peptidases. Gram-negative bacteria from the human gut microbiome encode a relative of the human endopeptidase inhibitor, α2-macroglobulin (α2M). Escherichia coli α2M (ECAM) is a ∼ 180-kDa multidomain membrane-anchored pan-peptidase inhibitor, which is cleaved by host endopeptidases in an accessible bait region. Structural studies by electron microscopy and crystallography reveal that this cleavage causes major structural rearrangement of more than half the 13-domain structure from a native to a compact induced form. It also exposes a reactive thioester bond, which covalently traps the peptidase. Subsequently, peptidase-laden ECAM is shed from the membrane and may dimerize. Trapped peptidases are still active except against very large substrates, so inhibition potentially prevents damage of large cell envelope components, but not host digestion. Mechanistically, these results document a novel monomeric "snap trap."
External links	Proc Natl Acad Sci U S A / PubMed:26100869 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.6 - 17.0 Å
Structure data	3016 5a42 EMDB-3016, PDB-5a42: Cryo-EM single particle 3D reconstruction of the native conformation of E. coli alpha-2-macroglobulin (ECAM) Method: EM (single particle) / Resolution: 16.0 Å EMDB-3017: Cryo-EM single particle 3D reconstruction of the trypsin-induced dimeric conformation of E. coli alpha-2-macroglobulin (ECAM) Method: EM (single particle) / Resolution: 14.5 Å EMDB-3018: Cryo-EM single particle 3D reconstruction of the induced, monomeric conformation of E. coli alpha-2-macroglobulin (ECAM) Method: EM (single particle) / Resolution: 17.0 Å PDB-4ziq: Crystal structure of trypsin activated alpha-2-macroglobulin from Escherichia coli. Method: X-RAY DIFFRACTION / Resolution: 2.55 Å PDB-4ziu: Crystal structure of native alpha-2-macroglobulin from Escherichia coli spanning the residues from domain MG7 to the C-terminus. Method: X-RAY DIFFRACTION / Resolution: 2.7 Å PDB-4zjg: Crystal structure of native alpha-2-macroglobulin from Escherichia coli spanning domains MG0-NIE-MG1. Method: X-RAY DIFFRACTION / Resolution: 2.3 Å PDB-4zjh: Crystal structure of native alpha-2-macroglobulin from Escherichia coli spanning domains NIE-MG1. Method: X-RAY DIFFRACTION / Resolution: 1.6 Å
Chemicals	ChemComp-GOL: GLYCEROL / Glycerol ChemComp-CL: Unknown entry / Chloride ChemComp-HOH: WATER / Water ChemComp-NI: NICKEL (II) ION / Nickel ChemComp-PG4: TETRAETHYLENE GLYCOL / precipitantYM / Polyethylene glycol ChemComp-PGE: TRIETHYLENE GLYCOL / Polyethylene glycol ChemComp-1PE: PENTAETHYLENE GLYCOL / precipitantYM / Polyethylene glycol ChemComp-PEG: DI(HYDROXYETHYL)ETHER / Diethylene glycol ChemComp-ACT: ACETATE ION / Acetate
Source	escherichia coli k-12 (bacteria) escherichia coli (strain k12) (bacteria)
Keywords	MEMBRANE PROTEIN / Bacterial pan-proteinase inhibitor / MEMBRANE PROTEIN/INHIBITOR / membrane protein and inhibitor complex / MEMBRANE PROTEIN-INHIBITOR complex / HYDROLASE INHIBITOR / PEPTIDASE INHIBITOR