[English] 日本語
Yorodumi
- EMDB-31087: LptB2FGC in complex with LPS from Klebsiella pneumoniae -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-31087
TitleLptB2FGC in complex with LPS from Klebsiella pneumoniae
Map data
Sample
  • Complex: LptB2FGC with LPS from Klebsiella pneumoniae
    • Protein or peptide: Lipopolysaccharide export system ATP-binding protein LptB
    • Protein or peptide: Lipopolysaccharide export system permease protein LptF
    • Protein or peptide: LPS export ABC transporter permease LptG
    • Protein or peptide: Lipopolysaccharide export system protein LptC
Function / homology
Function and homology information


ATPase-coupled transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex / transmembrane transport / hydrolase activity / ATP binding / cytoplasm
Similarity search - Function
Permease LptG/LptF-related / LPS export ABC transporter permease LptF / LPS export ABC transporter permease LptG / Lipopolysaccharide export system permease LptF/LptG / Branched-chain amino acid ATP-binding cassette transporter, C-terminal / Branched-chain amino acid ATP-binding cassette transporter / LPS export ABC transporter, ATP-binding protein LptB / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter ...Permease LptG/LptF-related / LPS export ABC transporter permease LptF / LPS export ABC transporter permease LptG / Lipopolysaccharide export system permease LptF/LptG / Branched-chain amino acid ATP-binding cassette transporter, C-terminal / Branched-chain amino acid ATP-binding cassette transporter / LPS export ABC transporter, ATP-binding protein LptB / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
LPS export ABC transporter permease LptG / Lipopolysaccharide export system permease protein LptF / Lipopolysaccharide export system ATP-binding protein LptB
Similarity search - Component
Biological speciesKlebsiella pneumoniae subsp. pneumoniae (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.85 Å
AuthorsLuo QS / Shi HG
Funding support China, 2 items
OrganizationGrant numberCountry
Chinese Academy of SciencesXDB37020201 China
National Natural Science Foundation of China (NSFC)31625009 China
CitationJournal: Biochem Biophys Res Commun / Year: 2021
Title: Cryo-EM structures of LptBFG and LptBFGC from Klebsiella pneumoniae in complex with lipopolysaccharide.
Authors: Qingshan Luo / Huigang Shi / Xueqing Xu /
Abstract: Lipopolysaccharide (LPS) is an essential component of the outer membrane (OM) in most Gram-negative bacteria. LPS transport from the inner membrane (IM) to the OM is achieved by seven ...Lipopolysaccharide (LPS) is an essential component of the outer membrane (OM) in most Gram-negative bacteria. LPS transport from the inner membrane (IM) to the OM is achieved by seven lipopolysaccharide transport proteins (LptA-G). LptBFG, an type VI ATP-binding cassette (ABC) transporter, forms a stable complex with LptC, extracts LPS from the IM and powers LPS transport to the OM. Here we report the cryo-EM structures of LptBFG and LptBFGC from Klebsiella pneumoniae in complex with LPS. The KpLptBFG-LPS structure provides detailed interactions between LPS and the transporter, while the KpLptBFGC-LPS structure may represent an intermediate state that the transmembrane helix of LptC has not been fully inserted into the transmembrane domains of LptBFG.
History
DepositionMar 22, 2021-
Header (metadata) releaseMar 2, 2022-
Map releaseMar 2, 2022-
UpdateMar 2, 2022-
Current statusMar 2, 2022Processing site: PDBj / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0172
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.0172
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_31087.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.04 Å
Density
Contour LevelBy AUTHOR: 0.0172 / Movie #1: 0.0172
Minimum - Maximum-0.05728113 - 0.0954283
Average (Standard dev.)-1.6712911e-05 (±0.0037128718)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions192192192
Spacing192192192
CellA=B=C: 199.68 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.041.041.04
M x/y/z192192192
origin x/y/z0.0000.0000.000
length x/y/z199.680199.680199.680
α/β/γ90.00090.00090.000
start NX/NY/NZ535455
NX/NY/NZ134138134
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS192192192
D min/max/mean-0.0570.095-0.000

-
Supplemental data

-
Mask #1

Fileemd_31087_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : LptB2FGC with LPS from Klebsiella pneumoniae

EntireName: LptB2FGC with LPS from Klebsiella pneumoniae
Components
  • Complex: LptB2FGC with LPS from Klebsiella pneumoniae
    • Protein or peptide: Lipopolysaccharide export system ATP-binding protein LptB
    • Protein or peptide: Lipopolysaccharide export system permease protein LptF
    • Protein or peptide: LPS export ABC transporter permease LptG
    • Protein or peptide: Lipopolysaccharide export system protein LptC

-
Supramolecule #1: LptB2FGC with LPS from Klebsiella pneumoniae

SupramoleculeName: LptB2FGC with LPS from Klebsiella pneumoniae / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Klebsiella pneumoniae subsp. pneumoniae (bacteria)
Recombinant expressionOrganism: Escherichia coli (E. coli)

-
Macromolecule #1: Lipopolysaccharide export system ATP-binding protein LptB

MacromoleculeName: Lipopolysaccharide export system ATP-binding protein LptB
type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
SequenceString: MATLTAKNLA KAYKGRRVVE DVSLTVNSGE IVGLLGPNGA GKTTTFYMVV GIVPRDAGNI IIDDEDISL LPLHARARRG IGYLPQEASI FRRLSVYDNL MAVLQIRDDL TSEQREDRAK E LMEEFHIE HLRDSLGQAL SGGERRRVEI ARALAANPKF ILLDEPFAGV ...String:
MATLTAKNLA KAYKGRRVVE DVSLTVNSGE IVGLLGPNGA GKTTTFYMVV GIVPRDAGNI IIDDEDISL LPLHARARRG IGYLPQEASI FRRLSVYDNL MAVLQIRDDL TSEQREDRAK E LMEEFHIE HLRDSLGQAL SGGERRRVEI ARALAANPKF ILLDEPFAGV DPISVIDIKR II EHLRDSG LGVLITDHNV RETLAVCERA YIVSQGHLIA HGTPQQILED EQVKRVYLGE DFR L

-
Macromolecule #2: Lipopolysaccharide export system permease protein LptF

MacromoleculeName: Lipopolysaccharide export system permease protein LptF
type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
SequenceString: MIIIRYLVRE TLKSQLAILF ILLLIFFCQK LVRILGAAVD GDIPTNLVLS LLGLGIPEMA QLILPLSLF LGLLMTLGKL YTESEITVMH ACGLSKAVLI KAAMILALFT GAVAAVNVMW A GPWSSRHQ DEVLAEAKAN PGMAALAQGQ FQQASDGNAV MFIESVNGNR ...String:
MIIIRYLVRE TLKSQLAILF ILLLIFFCQK LVRILGAAVD GDIPTNLVLS LLGLGIPEMA QLILPLSLF LGLLMTLGKL YTESEITVMH ACGLSKAVLI KAAMILALFT GAVAAVNVMW A GPWSSRHQ DEVLAEAKAN PGMAALAQGQ FQQASDGNAV MFIESVNGNR FHDVFLAQLR PK GNARPSV VVADSGELSQ QKDGSQVVTL NKGTRFEGTA MLRDFRITDF NNYQAIIGHQ AVS ADPDDT EQMDMRTLWK THTDRARAEL HWRFTLVATV FIMALMVVPL SVVNPRQGRV LSML PAMLL YLVFFLLQTS IKSNGGKGKM DPAIWMWAIN LLYFALAVLL NLWDTVPMRR FRARF NKGA A

-
Macromolecule #3: LPS export ABC transporter permease LptG

MacromoleculeName: LPS export ABC transporter permease LptG / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
SequenceString: MQAFGVLDRY IGKTIFNTIM MTLFMLVSLS GIIKFVDQLK KSGQGSYDAL GAGLYTILSV PKDIQIFFP MAALLGALLG LGMLAQRSEL VVMQASGFTR LQVALAVMKT AIPLVLLTMA I GEWVAPQG EQMARNYRAQ QMYGGSLLST QQGLWAKDGH NFVYIERVKG ...String:
MQAFGVLDRY IGKTIFNTIM MTLFMLVSLS GIIKFVDQLK KSGQGSYDAL GAGLYTILSV PKDIQIFFP MAALLGALLG LGMLAQRSEL VVMQASGFTR LQVALAVMKT AIPLVLLTMA I GEWVAPQG EQMARNYRAQ QMYGGSLLST QQGLWAKDGH NFVYIERVKG NDELGGVSIY AF NPERRLQ SVRYAASAKF DSENKVWRLS QVDESDLTDP KQVTGSQMVS GTWKTNLTPD KLG VVALDP DALSISGLHN YVKYLKSSGQ DPGRYQLNMW SKIFQPLSVA VMMLMALSFI FGPL RSVPM GVRVVTGISF GFIFYVLDQI FGPLTLVYGI PPIIGALLPS ASFFLISLWL MMRKA

-
Macromolecule #4: Lipopolysaccharide export system protein LptC

MacromoleculeName: Lipopolysaccharide export system protein LptC / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
SequenceString: MSKTRRWVII LLSLLALILI GLNLANTDDT AQPEVNPNDP TYKSEHTDTV VYSPEGALSY RLIAEHVEY FSDQEVSWFT KPVMTTFDTN KVPTWSVRAD KAKLTNDRML YLYGHVEVNA L APDSQLRK ITTDNAQINL VTQDVTSDDM VTLYGTTFNS SGLKMRGNLR ...String:
MSKTRRWVII LLSLLALILI GLNLANTDDT AQPEVNPNDP TYKSEHTDTV VYSPEGALSY RLIAEHVEY FSDQEVSWFT KPVMTTFDTN KVPTWSVRAD KAKLTNDRML YLYGHVEVNA L APDSQLRK ITTDNAQINL VTQDVTSDDM VTLYGTTFNS SGLKMRGNLR SKNAELIEKV RT SYEIQNK QTQP

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: NITROGEN / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: LEICA EM GP

-
Electron microscopy

MicroscopeFEI TITAN
Image recordingFilm or detector model: GATAN K2 BASE (4k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.4000000000000001 µm

+
Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.85 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 71000
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more