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- PDB-7fa0: The crystal structure of VyPAL2-C214A, a dead mutant of VyPAL2 pe... -

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Basic information

Entry
Database: PDB / ID: 7fa0
TitleThe crystal structure of VyPAL2-C214A, a dead mutant of VyPAL2 peptide asparaginyl ligase in form II
ComponentsPeptide Asparaginyl Ligases
KeywordsPLANT PROTEIN / AEP / PAL / Legumain / peptide ligase
Function / homology: / Legumain, prodomain / Legumain prodomain superfamily / Asparaginyl endopeptidase / Peptidase C13, legumain / Peptidase C13 family / proteolysis involved in protein catabolic process / cysteine-type endopeptidase activity / Peptide Asparaginyl Ligases
Function and homology information
Biological speciesViola philippica (plant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsHu, S. / Sahili, A. / Lescar, J.
Funding support Singapore, 1items
OrganizationGrant numberCountry
Ministry of Education (MoE, Singapore)MOE2016-T3-1-003 Singapore
CitationJournal: Plant Cell / Year: 2022
Title: Structural basis for proenzyme maturation, substrate recognition, and ligation by a hyperactive peptide asparaginyl ligase.
Authors: Hu, S. / El Sahili, A. / Kishore, S. / Wong, Y.H. / Hemu, X. / Goh, B.C. / Zhipei, S. / Wang, Z. / Tam, J.P. / Liu, C.F. / Lescar, J.
History
DepositionJul 5, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 13, 2022Provider: repository / Type: Initial release
Revision 1.1Nov 30, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Dec 14, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.name
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp_atom / chem_comp_bond / pdbx_validate_main_chain_plane / pdbx_validate_peptide_omega / pdbx_validate_rmsd_angle
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_label_atom_id / _pdbx_validate_rmsd_angle.angle_deviation / _pdbx_validate_rmsd_angle.angle_standard_deviation / _pdbx_validate_rmsd_angle.angle_target_value / _pdbx_validate_rmsd_angle.angle_value / _pdbx_validate_rmsd_angle.auth_atom_id_1 / _pdbx_validate_rmsd_angle.auth_atom_id_2 / _pdbx_validate_rmsd_angle.auth_atom_id_3 / _pdbx_validate_rmsd_angle.auth_comp_id_1 / _pdbx_validate_rmsd_angle.auth_comp_id_3 / _pdbx_validate_rmsd_angle.auth_seq_id_1 / _pdbx_validate_rmsd_angle.auth_seq_id_3
Revision 2.1Nov 29, 2023Group: Refinement description / Category: pdbx_initial_refinement_model
Revision 2.2May 1, 2024Group: Structure summary / Category: struct / Item: _struct.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Peptide Asparaginyl Ligases
B: Peptide Asparaginyl Ligases
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,8788
Polymers62,2022
Non-polymers1,6776
Water8,485471
1
A: Peptide Asparaginyl Ligases
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9114
Polymers31,1011
Non-polymers8103
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Peptide Asparaginyl Ligases
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9684
Polymers31,1011
Non-polymers8673
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)76.495, 78.546, 92.67
Angle α, β, γ (deg.)90, 90, 90
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Peptide Asparaginyl Ligases


Mass: 31100.783 Da / Num. of mol.: 2 / Mutation: C214A
Source method: isolated from a genetically manipulated source
Details: D171 (forming SNN), residue 172 is HD0 (HIS + SNN) / Source: (gene. exp.) Viola philippica (plant) / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: A0A509GV09
#2: Polysaccharide alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LFucpa1-6DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#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.: 1
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: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 471 / Source method: isolated from a natural source / Formula: H2O
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: 2.24 Å3/Da / Density % sol: 45.04 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / Details: 0.2 M Potassium formate, 20% PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.00001 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 3, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00001 Å / Relative weight: 1
ReflectionResolution: 1.8→46.33 Å / Num. obs: 51971 / % possible obs: 99.09 % / Redundancy: 6.7 % / Biso Wilson estimate: 27.28 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.09147 / Rpim(I) all: 0.03844 / Rrim(I) all: 0.09946 / Net I/σ(I): 12.65
Reflection shellResolution: 1.8→1.864 Å / Redundancy: 6.2 % / Rmerge(I) obs: 1.008 / Mean I/σ(I) obs: 2.12 / Num. unique obs: 5111 / CC1/2: 0.698 / CC star: 0.907 / Rpim(I) all: 0.4336 / Rrim(I) all: 1.1 / % possible all: 98.35

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Processing

Software
NameVersionClassification
BUSTER2.10.3refinement
autoPROCdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6IDV

6idv


Resolution: 1.8→46.33 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.953 / SU R Cruickshank DPI: 0.117 / Cross valid method: THROUGHOUT / SU R Blow DPI: 0.125 / SU Rfree Blow DPI: 0.111 / SU Rfree Cruickshank DPI: 0.107
RfactorNum. reflection% reflectionSelection details
Rfree0.1944 2618 -RANDOM
Rwork0.1636 ---
obs0.1688 51968 99.1 %-
Displacement parametersBiso mean: 33.24 Å2
Baniso -1Baniso -2Baniso -3
1--1.0547 Å20 Å20 Å2
2---0.5928 Å20 Å2
3---1.6475 Å2
Refine analyzeLuzzati coordinate error obs: 0.21 Å
Refinement stepCycle: LAST / Resolution: 1.8→46.33 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4270 0 124 471 4865
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0084546HARMONIC2
X-RAY DIFFRACTIONt_angle_deg0.966194HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d1534SINUSOIDAL2
X-RAY DIFFRACTIONt_gen_planes781HARMONIC5
X-RAY DIFFRACTIONt_it4546HARMONIC10
X-RAY DIFFRACTIONt_chiral_improper_torsion621SEMIHARMONIC5
X-RAY DIFFRACTIONt_ideal_dist_contact4220SEMIHARMONIC4
X-RAY DIFFRACTIONt_omega_torsion3.59
X-RAY DIFFRACTIONt_other_torsion15.31
LS refinement shellResolution: 1.8→1.81 Å
RfactorNum. reflection% reflection
Rfree0.2928 58 -
Rwork0.2047 --
obs0.2094 1040 98.14 %
Refinement TLS params.

Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.33450.1709-0.38381.2669-0.44671.01690.0688-0.0355-0.0076-0.03550.0269-0.0683-0.0076-0.0683-0.0957-0.0860.01370.0191-0.0990.0127-0.0613-3.5334-8.2454-8.8859
22.42620.5078-0.12611.7368-0.38471.41360.01840.1152-0.140.1152-0.07440.1142-0.140.11420.056-0.0894-0.0044-0.0071-0.10150.0059-0.1063-41.35958.3257-11.2416
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{ A|* }
2X-RAY DIFFRACTION2{ B|* }

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