[English] 日本語
Yorodumi
- EMDB-16913: Structure of the MlaCD complex (2:6 stoichiometry) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-16913
TitleStructure of the MlaCD complex (2:6 stoichiometry)
Map data
Sample
  • Complex: MlaCD (2:6 stoichiometry)
    • Protein or peptide: ABC transporter substrate-binding protein
    • Protein or peptide: ABC-type organic solvent transporter
KeywordsOuter membrane / phospholipids / gram-negative bacteria / lipid transport
Function / homology
Function and homology information


phospholipid transporter activity / phospholipid binding / extracellular region
Similarity search - Function
Tgt2/MlaC superfamily / Toluene tolerance Ttg2/phospholipid-binding protein MlaC / MlaC protein / Probable phospholipid ABC transporter-binding protein MlaD / Mce/MlaD / MlaD protein
Similarity search - Domain/homology
ABC-type organic solvent transporter / ABC transporter substrate-binding protein
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.38 Å
AuthorsWotherspoon P / Bui S / Sridhar P / Bergeron JRC / Knowles TJ
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Biotechnology and Biological Sciences Research Council (BBSRC) United Kingdom
CitationJournal: To Be Published
Title: The structure of the MlaC-MlaD complex reveals novel insights into periplasmic phospholipid transport processes
Authors: Wotherspoon P / Bui S / Sridhar P / Ratkeviciute G / Colburn J / Johnston H / Cooper BF / Bryant JA / Hughes GW / Stransfeld PJ / Bergeron JRC / Knowles TJ
History
DepositionMar 24, 2023-
Header (metadata) releaseJul 10, 2024-
Map releaseJul 10, 2024-
UpdateJul 10, 2024-
Current statusJul 10, 2024Processing site: PDBe / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_16913.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.71 Å
Density
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.29244334 - 0.43565294
Average (Standard dev.)0.0010002712 (±0.012610169)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions350350350
Spacing350350350
CellA=B=C: 248.5 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Sample components

-
Entire : MlaCD (2:6 stoichiometry)

EntireName: MlaCD (2:6 stoichiometry)
Components
  • Complex: MlaCD (2:6 stoichiometry)
    • Protein or peptide: ABC transporter substrate-binding protein
    • Protein or peptide: ABC-type organic solvent transporter

-
Supramolecule #1: MlaCD (2:6 stoichiometry)

SupramoleculeName: MlaCD (2:6 stoichiometry) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #2, #1
Source (natural)Organism: Escherichia coli (E. coli)

-
Macromolecule #1: ABC-type organic solvent transporter

MacromoleculeName: ABC-type organic solvent transporter / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 19.593133 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MQTKKNEIWV GIFLLAALLA ALFVCLKAAN VTSIRTEPTY TLYATFDNIG GLKARSPVSI GGVVVGRVAD ITLDPKTYLP RVTLEIEQR YNHIPDTSSL SIRTSGLLGE QYLALNVGFE DPELGTAILK DGDTIQDTKS AMVLEDLIGQ FLYGSKGDDN K NSGDAPAA APGNNETTEP VGTTK

UniProtKB: ABC-type organic solvent transporter

-
Macromolecule #2: ABC transporter substrate-binding protein

MacromoleculeName: ABC transporter substrate-binding protein / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 23.989559 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MFKRLMMVAL LVIAPLSAAT AADQTNPYKL MDEAAQKTFD RLKNEQPQIR ANPDYLRTIV DQELLPYVQV KYAGALVLGQ YYKSATPAQ REAYFAAFRE YLKQAYGQAL AMYHGQTYQI APEQPLGDKT IVPIRVTIID PNGRPPVRLD FQWRKNSQTG N WQAYDMIA ...String:
MFKRLMMVAL LVIAPLSAAT AADQTNPYKL MDEAAQKTFD RLKNEQPQIR ANPDYLRTIV DQELLPYVQV KYAGALVLGQ YYKSATPAQ REAYFAAFRE YLKQAYGQAL AMYHGQTYQI APEQPLGDKT IVPIRVTIID PNGRPPVRLD FQWRKNSQTG N WQAYDMIA EGVSMITTKQ NEWGTLLRTK GIDGLTAQLK SISQQKITLE EKK

UniProtKB: ABC transporter substrate-binding protein

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 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: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.38 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 58259
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

+
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