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- PDB-6inu: Crystal structure of the CysR-CTLD2 fragment of human MR at acidi... -

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Basic information

Entry
Database: PDB / ID: 6inu
TitleCrystal structure of the CysR-CTLD2 fragment of human MR at acidic pH (pH 4.6)
ComponentsMacrophage mannose receptor 1
KeywordsIMMUNE SYSTEM / CD206 / mannose receptor family / pH-dependent / conformational change / scavenger receptor
Function / homology
Function and homology information


cargo receptor activity / Cross-presentation of soluble exogenous antigens (endosomes) / D-mannose binding / cellular response to interleukin-4 / receptor-mediated endocytosis / cellular response to type II interferon / Modulation by Mtb of host immune system / transmembrane signaling receptor activity / signaling receptor activity / cellular response to lipopolysaccharide ...cargo receptor activity / Cross-presentation of soluble exogenous antigens (endosomes) / D-mannose binding / cellular response to interleukin-4 / receptor-mediated endocytosis / cellular response to type II interferon / Modulation by Mtb of host immune system / transmembrane signaling receptor activity / signaling receptor activity / cellular response to lipopolysaccharide / virus receptor activity / endosome membrane / cell surface / plasma membrane
Similarity search - Function
MRC2-like, N-terminal cysteine-rich domain / Fibronectin type II domain / Fibronectin type II domain superfamily / Fibronectin type II domain / Fibronectin type-II collagen-binding domain signature. / Fibronectin type-II collagen-binding domain profile. / Fibronectin type 2 domain / : / Ricin-type beta-trefoil lectin domain / C-type lectin, conserved site ...MRC2-like, N-terminal cysteine-rich domain / Fibronectin type II domain / Fibronectin type II domain superfamily / Fibronectin type II domain / Fibronectin type-II collagen-binding domain signature. / Fibronectin type-II collagen-binding domain profile. / Fibronectin type 2 domain / : / Ricin-type beta-trefoil lectin domain / C-type lectin, conserved site / C-type lectin domain signature. / Ricin-type beta-trefoil / Mannose-Binding Protein A; Chain A / Mannose-Binding Protein A, subunit A / Lectin domain of ricin B chain profile. / Ricin B, lectin domain / Ricin B-like lectins / Lectin C-type domain / C-type lectin domain profile. / C-type lectin-like / C-type lectin (CTL) or carbohydrate-recognition domain (CRD) / C-type lectin-like/link domain superfamily / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / C-type lectin fold / Kringle-like fold / Roll / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Macrophage mannose receptor 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.65 Å
AuthorsHu, Z. / He, Y.
Funding support China, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China31270772 China
Chinese Academy of SciencesXDB08020102 China
CitationJournal: J.Struct.Biol. / Year: 2019
Title: Structural basis of the pH-dependent conformational change of the N-terminal region of human mannose receptor/CD206.
Authors: Hu, Z. / Wang, Y. / Cheng, C. / He, Y.
History
DepositionOct 27, 2018Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 18, 2019Provider: repository / Type: Initial release
Revision 1.1Dec 11, 2019Group: Database references / Category: citation / Item: _citation.journal_volume
Revision 1.2Mar 25, 2020Group: Database references / Category: citation / Item: _citation.page_first / _citation.page_last
Revision 1.3Nov 22, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Oct 9, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Macrophage mannose receptor 1
B: Macrophage mannose receptor 1


Theoretical massNumber of molelcules
Total (without water)108,8262
Polymers108,8262
Non-polymers00
Water00
1
A: Macrophage mannose receptor 1


Theoretical massNumber of molelcules
Total (without water)54,4131
Polymers54,4131
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Macrophage mannose receptor 1


Theoretical massNumber of molelcules
Total (without water)54,4131
Polymers54,4131
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)238.763, 74.122, 109.968
Angle α, β, γ (deg.)90.00, 114.74, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Macrophage mannose receptor 1 / MMR / C-type lectin domain family 13 member D / C-type lectin domain family 13 member D-like / ...MMR / C-type lectin domain family 13 member D / C-type lectin domain family 13 member D-like / Human mannose receptor / hMR / Macrophage mannose receptor 1-like protein 1


Mass: 54412.914 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MRC1, CLEC13D, CLEC13DL, MRC1L1 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P22897
Has protein modificationY

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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: 4.06 Å3/Da / Density % sol: 69.71 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, sitting drop
Details: 0.01 M cobalt chloride hexahydrate, 0.1 M sodium acetate trihydrate (pH 4.6), 1.0 M 1,6-Hexanediol

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Data collection

DiffractionMean temperature: 80 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NFPSS / Beamline: BL18U / Wavelength: 0.98 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Dec 29, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.65→30 Å / Num. obs: 50653 / % possible obs: 99.4 % / Redundancy: 5.2 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 17.8
Reflection shellResolution: 2.65→2.74 Å / Rmerge(I) obs: 0.409 / Num. unique obs: 4940

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
HKL-3000data reduction
HKL-3000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5XTS

5xts


Resolution: 2.65→29.57 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.4 / Phase error: 29.91
RfactorNum. reflection% reflection
Rfree0.258 1994 3.94 %
Rwork0.2147 --
obs0.2164 50596 99.14 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.65→29.57 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7187 0 0 0 7187
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.017406
X-RAY DIFFRACTIONf_angle_d0.94910053
X-RAY DIFFRACTIONf_dihedral_angle_d11.624367
X-RAY DIFFRACTIONf_chiral_restr0.0581036
X-RAY DIFFRACTIONf_plane_restr0.0071271
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6494-2.71560.42741320.3473312X-RAY DIFFRACTION96
2.7156-2.7890.37371380.32583390X-RAY DIFFRACTION98
2.789-2.8710.31341460.30783460X-RAY DIFFRACTION99
2.871-2.96360.33171400.27713466X-RAY DIFFRACTION100
2.9636-3.06940.28141430.26543463X-RAY DIFFRACTION99
3.0694-3.19220.31291440.26043456X-RAY DIFFRACTION100
3.1922-3.33730.27891380.25353490X-RAY DIFFRACTION100
3.3373-3.51290.26971440.23463458X-RAY DIFFRACTION100
3.5129-3.73260.27461450.21383456X-RAY DIFFRACTION99
3.7326-4.02020.26461380.20133527X-RAY DIFFRACTION100
4.0202-4.42360.2461460.17613491X-RAY DIFFRACTION100
4.4236-5.06090.19661490.16293502X-RAY DIFFRACTION100
5.0609-6.36570.22181430.18553534X-RAY DIFFRACTION100
6.3657-29.57180.21751480.19293597X-RAY DIFFRACTION99

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