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- EMDB-24233: The cryoEM structure of LbpB from N. gonorrhoeae in complex with ... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-24233 | |||||||||
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Title | The cryoEM structure of LbpB from N. gonorrhoeae in complex with lactoferrin | |||||||||
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Function / homology | ![]() negative regulation by host of viral process / membrane destabilizing activity / Mtb iron assimilation by chelation / phagocytic vesicle lumen / positive regulation of toll-like receptor 4 signaling pathway / Metal sequestration by antimicrobial proteins / negative regulation of viral process / negative regulation of cysteine-type endopeptidase activity / negative regulation of tumor necrosis factor (ligand) superfamily member 11 production / negative regulation of single-species biofilm formation in or on host organism ...negative regulation by host of viral process / membrane destabilizing activity / Mtb iron assimilation by chelation / phagocytic vesicle lumen / positive regulation of toll-like receptor 4 signaling pathway / Metal sequestration by antimicrobial proteins / negative regulation of viral process / negative regulation of cysteine-type endopeptidase activity / negative regulation of tumor necrosis factor (ligand) superfamily member 11 production / negative regulation of single-species biofilm formation in or on host organism / positive regulation of bone mineralization involved in bone maturation / negative regulation of lipopolysaccharide-mediated signaling pathway / specific granule / negative regulation of osteoclast development / antifungal humoral response / positive regulation of chondrocyte proliferation / negative regulation of ATP-dependent activity / regulation of tumor necrosis factor production / bone morphogenesis / Antimicrobial peptides / cysteine-type endopeptidase inhibitor activity / negative regulation of viral genome replication / positive regulation of osteoblast proliferation / humoral immune response / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / positive regulation of osteoblast differentiation / regulation of cytokine production / protein serine/threonine kinase activator activity / ossification / innate immune response in mucosa / secretory granule / lipopolysaccharide binding / cell outer membrane / positive regulation of protein serine/threonine kinase activity / recycling endosome / specific granule lumen / antimicrobial humoral immune response mediated by antimicrobial peptide / tertiary granule lumen / positive regulation of NF-kappaB transcription factor activity / heparin binding / iron ion transport / antibacterial humoral response / positive regulation of canonical NF-kappaB signal transduction / defense response to Gram-negative bacterium / killing of cells of another organism / early endosome / iron ion binding / Amyloid fiber formation / serine-type endopeptidase activity / Neutrophil degranulation / negative regulation of apoptotic process / cell surface / protein-containing complex / proteolysis / DNA binding / extracellular space / extracellular exosome / extracellular region / nucleus / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
![]() | Yadav R / Noinaj N | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insight into the dual function of LbpB in mediating Neisserial pathogenesis. Authors: Ravi Yadav / Srinivas Govindan / Courtney Daczkowski / Andrew Mesecar / Srinivas Chakravarthy / Nicholas Noinaj / ![]() Abstract: Lactoferrin-binding protein B (LbpB) is a lipoprotein present on the surface of that has been postulated to serve dual functions during pathogenesis in both iron acquisition from lactoferrin (Lf), ...Lactoferrin-binding protein B (LbpB) is a lipoprotein present on the surface of that has been postulated to serve dual functions during pathogenesis in both iron acquisition from lactoferrin (Lf), and in providing protection against the cationic antimicrobial peptide lactoferricin (Lfcn). While previous studies support a dual role for LbpB, exactly how these ligands interact with LbpB has remained unknown. Here, we present the structures of LbpB from and in complex with human holo-Lf, forming a 1:1 complex and confirmed by size-exclusion chromatography small-angle X-ray scattering. LbpB consists of N- and C-lobes with the N-lobe interacting extensively with the C-lobe of Lf. Our structures provide insight into LbpB's preference towards holo-Lf, and our mutagenesis and binding studies show that Lf and Lfcn bind independently. Our studies provide the molecular details for how LbpB serves to capture and preserve Lf in an iron-bound state for delivery to the membrane transporter LbpA for iron piracy, and as an antimicrobial peptide sink to evade host immune defenses. | |||||||||
History |
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Structure visualization
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13 KB 13 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.9 KB | Display | ![]() |
Images | ![]() | 65.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 439.8 KB | Display | ![]() |
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Full document | ![]() | 439.3 KB | Display | |
Data in XML | ![]() | 10.9 KB | Display | |
Data in CIF | ![]() | 14.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7n88MC ![]() 7jrdC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : complex between lactoferrin binding protein and lactoferrin
Entire | Name: complex between lactoferrin binding protein and lactoferrin |
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Components |
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-Supramolecule #1: complex between lactoferrin binding protein and lactoferrin
Supramolecule | Name: complex between lactoferrin binding protein and lactoferrin type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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-Supramolecule #2: lactoferrin binding protein
Supramolecule | Name: lactoferrin binding protein / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Supramolecule #3: lactoferrin
Supramolecule | Name: lactoferrin / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Macromolecule #1: Lactoferrin-binding protein B
Macromolecule | Name: Lactoferrin-binding protein B / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 78.432734 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GAMGGNFGVQ PVVESTPTAY PVTFKSKDVP TSPPPAEPSV ETTPVNRPAV GAAMRLLRRN TAFHREDGTA IPDSKQAEEK LSFKEGDVL FLYGSKGNKL QQLKSEIHKR DSDVEIRTSE KENKKYGYEF VDAGYVYTKN GKDEIEQNSG GKRFTHRFGY D GFVYYSGE ...String: GAMGGNFGVQ PVVESTPTAY PVTFKSKDVP TSPPPAEPSV ETTPVNRPAV GAAMRLLRRN TAFHREDGTA IPDSKQAEEK LSFKEGDVL FLYGSKGNKL QQLKSEIHKR DSDVEIRTSE KENKKYGYEF VDAGYVYTKN GKDEIEQNSG GKRFTHRFGY D GFVYYSGE RPSQSLPSAG TVKYFGNWQY MTDAKRHRTG KAVASDDLGY ITFYGNDIGA TSYAAKDADD REKHPAEYTV DF DKKILKG ELIKNQYVQK KNDPKKPLTI YNITADLNGN RFTGSAKVNT EVKTRHADKE YLFFHTDADQ RLEGGFFGDN GEE LAGRFI SNDNGVFGVF AGKQKTNASG TNPAMPFGKH TKILDSLKIS VDEATDENPR PFEVSTMPDF GHPDKLLVEG REIP LVSKE KTIDLADGRK MTVSACCDFL TYVKLGRIKT ERPAVKPKAQ DEEDSGINNG EESEDEEEIA EESEDEVSED DNGED EDEI VEEEADEAEE IEEEAEEEEP EEESPEEGNG VSDGIPPAPE ALKGRDIDLF LKGIRTAEAD IPKTGTAHYT GTWEAR IGE PIQWDNKADK AAKAEFDVDF GNKSISGTLT EQNGVEPAFR IENGVIEGNG FHATARTRDN GINLSGNGST NPQSFKA DN LLVTGGFYGP QAAELGGTIF NKDGKSLGIT EDIENEVENE ADVGEQLEPE VKPQFGVVFG AKKDNKEVEK |
-Macromolecule #2: Lactotransferrin
Macromolecule | Name: Lactotransferrin / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO EC number: Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 76.263266 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GRRRSVQWCA VSQPEATKCF QWQRNMRKVR GPPVSCIKRD SPIQCIQAIA ENRADAVTLD GGFIYEAGLA PYKLRPVAAE VYGTERQPR THYYAVAVVK KGGSFQLNEL QGLKSCHTGL RRTAGWNVPI GTLRPFLNWT GPPEPIEAAV ARFFSASCVP G ADKGQFPN ...String: GRRRSVQWCA VSQPEATKCF QWQRNMRKVR GPPVSCIKRD SPIQCIQAIA ENRADAVTLD GGFIYEAGLA PYKLRPVAAE VYGTERQPR THYYAVAVVK KGGSFQLNEL QGLKSCHTGL RRTAGWNVPI GTLRPFLNWT GPPEPIEAAV ARFFSASCVP G ADKGQFPN LCRLCAGTGE NKCAFSSQEP YFSYSGAFKC LRDGAGDVAF IRESTVFEDL SDEAERDEYE LLCPDNTRKP VD KFKDCHL ARVPSHAVVA RSVNGKEDAI WNLLRQAQEK FGKDKSPKFQ LFGSPSGQKD LLFKDSAIGF SRVPPRIDSG LYL GSGYFT AIQNLRKSEE EVAARRARVV WCAVGEQELR KCNQWSGLSE GSVTCSSAST TEDCIALVLK GEADAMSLDG GYVY TAGKC GLVPVLAENY KSQQSSDPDP NCVDRPVEGY LAVAVVRRSD TSLTWNSVKG KKSCHTAVDR TAGWNIPMGL LFNQT GSCK FDEYFSQSCA PGSDPRSNLC ALCIGDEQGE NKCVPNSNER YYGYTGAFRC LAENAGDVAF VKDVTVLQNT DGNNNE AWA KDLKLADFAL LCLDGKRKPV TEARSCHLAM APNHAVVSRM DKVERLKQVL LHQQAKFGRN GSDCPDKFCL FQSETKN LL FNDNTECLAR LHGKTTYEKY LGPQYVAGIT NLKKCSTSPL LEACEFLRK |
-Macromolecule #3: FE (III) ION
Macromolecule | Name: FE (III) ION / type: ligand / ID: 3 / Number of copies: 2 / Formula: FE |
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Molecular weight | Theoretical: 55.845 Da |
-Macromolecule #4: BICARBONATE ION
Macromolecule | Name: BICARBONATE ION / type: ligand / ID: 4 / Number of copies: 2 / Formula: BCT |
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Molecular weight | Theoretical: 61.017 Da |
Chemical component information | ![]() ChemComp-BCT: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 53.68 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |