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- PDB-8j5u: Crystal structure of Mycobacterium tuberculosis OppA complexed wi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8j5u | |||||||||
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Title | Crystal structure of Mycobacterium tuberculosis OppA complexed with an endogenous oligopeptide | |||||||||
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![]() | PEPTIDE BINDING PROTEIN / OppA / Oligopeptide binding protein / Cluster C SBP / Mycobacterium tuberculosis | |||||||||
Function / homology | ![]() Tolerance by Mtb to nitric oxide produced by macrophages / glutathione binding / peptide transport / protein import / peptide transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex / peptide binding / outer membrane-bounded periplasmic space / periplasmic space / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Yang, X. / Hu, T. / Zhang, B. / Rao, Z. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: An oligopeptide permease, OppABCD, requires an iron-sulfur cluster domain for functionality. Authors: Xiaolin Yang / Tianyu Hu / Jingxi Liang / Zhiqi Xiong / Zhenli Lin / Yao Zhao / Xiaoting Zhou / Yan Gao / Shan Sun / Xiuna Yang / Luke W Guddat / Haitao Yang / Zihe Rao / Bing Zhang / ![]() ![]() Abstract: Oligopeptide permease, OppABCD, belongs to the type I ABC transporter family. Its role is to import oligopeptides into bacteria for nutrient uptake and to modulate the host immune response. OppABCD ...Oligopeptide permease, OppABCD, belongs to the type I ABC transporter family. Its role is to import oligopeptides into bacteria for nutrient uptake and to modulate the host immune response. OppABCD consists of a cluster C substrate-binding protein (SBP), OppA, membrane-spanning OppB and OppC subunits, and an ATPase, OppD, that contains two nucleotide-binding domains (NBDs). Here, using cryo-electron microscopy, we determined the high-resolution structures of Mycobacterium tuberculosis OppABCD in the resting state, oligopeptide-bound pre-translocation state, AMPPNP-bound pre-catalytic intermediate state and ATP-bound catalytic intermediate state. The structures show an assembly of a cluster C SBP with its ABC translocator and a functionally required [4Fe-4S] cluster-binding domain in OppD. Moreover, the ATP-bound OppABCD structure has an outward-occluded conformation, although no substrate was observed in the transmembrane cavity. Here, we reveal an oligopeptide recognition and translocation mechanism of OppABCD, which provides a perspective on how this and other type I ABC importers facilitate bulk substrate transfer across the lipid bilayer. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.9 KB | Display | ![]() |
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PDB format | ![]() | 90.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 423.5 KB | Display | ![]() |
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Full document | ![]() | 426.9 KB | Display | |
Data in XML | ![]() | 21.9 KB | Display | |
Data in CIF | ![]() | 32 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8j5qC ![]() 8j5rC ![]() 8j5sC ![]() 8j5tC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 64609.340 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Author stated: The data collection statistics was calculated within the same resolution range as the refinement. The number of collected unique reflections was 39151. After anisotropic ...Details: Author stated: The data collection statistics was calculated within the same resolution range as the refinement. The number of collected unique reflections was 39151. After anisotropic correction using the STARANISO server and refinement using PHENIX, the number of unique reflections was 29132. Source: (gene. exp.) ![]() Gene: Rv1280c, MTCY50.02 Production host: ![]() References: UniProt: P9WGU5 |
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#2: Protein/peptide | Mass: 913.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.21 % |
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Crystal grow | Temperature: 289.15 K / Method: vapor diffusion, sitting drop Details: 100 mM HEPES (pH 7.5), 24% (w/v) polyethylene glycol 1500 (PEG1500), 200 mM L-proline. |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 9, 2022 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9785 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.98→50 Å / Num. obs: 39151 / % possible obs: 99.5 % / Redundancy: 6.4 % / CC1/2: 0.997 / Rmerge(I) obs: 0.135 / Rrim(I) all: 0.146 / Net I/σ(I): 10.51 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 1.98→48.88 Å
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LS refinement shell | Resolution: 1.98→2.03 Å
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