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- PDB-7p8j: Receptor-binding domain (RBD) of the spike protein of the bat cor... -

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Basic information

Entry
Database: PDB / ID: 7p8j
TitleReceptor-binding domain (RBD) of the spike protein of the bat coronavirus RaTG13 virus in complex with the extracellular domain of human angiotensin-converting enzyme 2 (ACE2) - Crystal form 2
Components
  • Processed angiotensin-converting enzyme 2
  • Spike glycoprotein
KeywordsCELL INVASION / COVID-19 / Bat coronavirus / Spillover / Zoonotic viral infection / Evolution
Function / homology
Function and homology information


positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / positive regulation of gap junction assembly / regulation of vasoconstriction / regulation of cardiac conduction ...positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / positive regulation of gap junction assembly / regulation of vasoconstriction / regulation of cardiac conduction / peptidyl-dipeptidase activity / maternal process involved in female pregnancy / angiotensin maturation / Metabolism of Angiotensinogen to Angiotensins / metallocarboxypeptidase activity / carboxypeptidase activity / negative regulation of signaling receptor activity / Attachment and Entry / positive regulation of cardiac muscle contraction / regulation of cytokine production / viral life cycle / blood vessel diameter maintenance / brush border membrane / regulation of transmembrane transporter activity / negative regulation of smooth muscle cell proliferation / endocytosis involved in viral entry into host cell / negative regulation of ERK1 and ERK2 cascade / cilium / metallopeptidase activity / endocytic vesicle membrane / positive regulation of reactive oxygen species metabolic process / virus receptor activity / regulation of cell population proliferation / regulation of inflammatory response / endopeptidase activity / Induction of Cell-Cell Fusion / Potential therapeutics for SARS / entry receptor-mediated virion attachment to host cell / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated endocytosis of virus by host cell / membrane fusion / Attachment and Entry / receptor-mediated virion attachment to host cell / symbiont entry into host cell / membrane raft / apical plasma membrane / endoplasmic reticulum lumen / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / host cell plasma membrane / virion membrane / cell surface / extracellular space / zinc ion binding / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane
Similarity search - Function
Collectrin-like domain profile. / Collectrin domain / Renal amino acid transporter / Peptidase family M2 domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Neutral zinc metallopeptidases, zinc-binding region signature. / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Spike glycoprotein, N-terminal domain superfamily ...Collectrin-like domain profile. / Collectrin domain / Renal amino acid transporter / Peptidase family M2 domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Neutral zinc metallopeptidases, zinc-binding region signature. / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / Spike glycoprotein, betacoronavirus / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus / Betacoronavirus spike glycoprotein S1, receptor binding / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like / Betacoronavirus-like spike glycoprotein S1, N-terminal / Spike glycoprotein S2, coronavirus, heptad repeat 1 / Spike glycoprotein S2, coronavirus, heptad repeat 2 / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile. / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile. / Spike glycoprotein S2 superfamily, coronavirus / Spike glycoprotein S2, coronavirus / Coronavirus spike glycoprotein S2 / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal
Similarity search - Domain/homology
Spike glycoprotein / Angiotensin-converting enzyme 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Bat coronavirus RaTG13
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 6.585 Å
AuthorsScietti, L. / Castelli, M. / Faravelli, S. / Clementi, N. / Mancini, N. / Forneris, F.
Funding support Italy, United States, Switzerland, Japan, Belgium, 7items
OrganizationGrant numberCountry
Italian Association for Cancer ResearchMFAG 20075 Italy
Italian Ministry of EducationPRIN 2017 2017RPHBCW_001 Italy
Italian Ministry of EducationDepartment of Excellence 2018-2022 Italy
Other privateGiovanni Armenise-Harvard Foundation Career Development Award CDA2013 United States
Other privateVelux Stiftung Opthalmology Grant id. 1375 Switzerland
Other privateMizutani Foundation For Glycoscience Grant id. 200039 Japan
Other governmentNATO Science for Peace and Security Program Grant id. G5701 Belgium
CitationJournal: To Be Published
Title: Constrained Evolution of SARS-CoV-2 Spike in Rhinolophus affinis Bats
Authors: Castelli, M. / Scietti, L. / Faravelli, S. / Clementi, N. / Forneris, F. / Mancini, N.
History
DepositionJul 22, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 3, 2022Provider: repository / Type: Initial release
Revision 1.1Aug 16, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Revision 1.2Jan 31, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Processed angiotensin-converting enzyme 2
B: Spike glycoprotein
C: Processed angiotensin-converting enzyme 2
D: Spike glycoprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)196,77014
Polymers191,5534
Non-polymers5,21710
Water00
1
A: Processed angiotensin-converting enzyme 2
B: Spike glycoprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)98,3857
Polymers95,7772
Non-polymers2,6085
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Processed angiotensin-converting enzyme 2
D: Spike glycoprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)98,3857
Polymers95,7772
Non-polymers2,6085
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)89.900, 107.717, 251.754
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain C
12chain B
22chain D

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain AA19 - 1547
211chain CC19 - 1547
112chain BB334 - 1345
212chain DD334 - 1345

NCS ensembles :
ID
1
2

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Components

#1: Protein Processed angiotensin-converting enzyme 2


Mass: 69511.039 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: Initial GS and final AAA sequences were introduced by molecular cloning
Source: (gene. exp.) Homo sapiens (human) / Gene: ACE2, UNQ868/PRO1885 / Plasmid: pUPE.06.45 / Details (production host): N-term His-Strep-TEV / Cell line (production host): HEK293F / Production host: Homo sapiens (human) / References: UniProt: Q9BYF1
#2: Protein Spike glycoprotein / S glycoprotein / E2 / Peplomer protein


Mass: 26265.598 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: cloning artifacts: GS sequence at the N-terminus and AA sequence at the C-terminus, + 6xHis-tag at the C-terminus
Source: (gene. exp.) Bat coronavirus RaTG13 / Plasmid: pCAGGS / Cell line (production host): HEK293F / Production host: Homo sapiens (human) / References: UniProt: A0A6B9WHD3
#3: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#4: Polysaccharide
beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.18 Å3/Da / Density % sol: 61.34 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.9
Details: 0.2-0.25 M sodium thiocyanate, 18-23% PEG 3350, pH 6.9

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 13, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 6.5→66.42 Å / Num. obs: 5280 / % possible obs: 99.7 % / Redundancy: 8.5 % / CC1/2: 0.979 / Rmerge(I) obs: 0.459 / Net I/σ(I): 2.8
Reflection shellResolution: 6.5→7.26 Å / Redundancy: 8.9 % / Rmerge(I) obs: 2.905 / Mean I/σ(I) obs: 0.4 / Num. unique obs: 1424 / CC1/2: 0.531 / % possible all: 99.2

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Processing

Software
NameVersionClassification
PHENIX1.16_3549refinement
PDB_EXTRACT3.27data extraction
xia2data reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6VW1

6vw1


Resolution: 6.585→49.516 Å / SU ML: 0.89 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 34.86 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.345 145 5.51 %
Rwork0.3179 2486 -
obs0.3195 2631 52.83 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 30 Å2 / Biso mean: 30 Å2 / Biso min: 30 Å2
Refinement stepCycle: final / Resolution: 6.585→49.516 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12790 0 346 0 13136
Biso mean--30 --
Num. residues----1580
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3748X-RAY DIFFRACTION0.486TORSIONAL
12C3748X-RAY DIFFRACTION0.486TORSIONAL
21B1212X-RAY DIFFRACTION0.486TORSIONAL
22D1212X-RAY DIFFRACTION0.486TORSIONAL
LS refinement shellResolution: 6.5855→49.516 Å / Rfactor Rfree error: 0
RfactorNum. reflection% reflection
Rfree0.345 145 -
Rwork0.3179 2486 -
obs--53 %

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