[English] 日本語
Yorodumi
- EMDB-44171: Mycolicibacterium smegmatis MmpL5 structure -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-44171
TitleMycolicibacterium smegmatis MmpL5 structure
Map dataMycolicibacterium smegmatis MmpL5 structure
Sample
  • Complex: MmpL5
    • Protein or peptide: MmpL5 protein
KeywordsMycolicibacterium smegmatis / siderophore / MmpL5 / TRANSPORT PROTEIN
Function / homologyMembrane transport protein MmpL family / : / Membrane transport protein MMPL domain / MMPL family / plasma membrane / MmpL5 protein
Function and homology information
Biological speciesMycolicibacterium smegmatis (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsMaharjan R / Klenotic PA / Zhang Z / Yu EW
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI145069 United States
CitationJournal: PLoS Biol / Year: 2024
Title: Structures of the mycobacterial MmpL4 and MmpL5 transporters provide insights into their role in siderophore export and iron acquisition.
Authors: Rakesh Maharjan / Zhemin Zhang / Philip A Klenotic / William D Gregor / Marios L Tringides / Meng Cui / Georgiana E Purdy / Edward W Yu /
Abstract: The Mycobacterium tuberculosis (Mtb) pathogen, the causative agent of the airborne infection tuberculosis (TB), harbors a number of mycobacterial membrane protein large (MmpL) transporters. These ...The Mycobacterium tuberculosis (Mtb) pathogen, the causative agent of the airborne infection tuberculosis (TB), harbors a number of mycobacterial membrane protein large (MmpL) transporters. These membrane proteins can be separated into 2 distinct subclasses, where they perform important functional roles, and thus, are considered potential drug targets to combat TB. Previously, we reported both X-ray and cryo-EM structures of the MmpL3 transporter, providing high-resolution structural information for this subclass of the MmpL proteins. Currently, there is no structural information available for the subclass associated with MmpL4 and MmpL5, transporters that play a critical role in iron homeostasis of the bacterium. Here, we report cryo-EM structures of the M. smegmatis MmpL4 and MmpL5 transporters to resolutions of 2.95 Å and 3.00 Å, respectively. These structures allow us to propose a plausible pathway for siderophore translocation via these 2 transporters, an essential step for iron acquisition that enables the survival and replication of the mycobacterium.
History
DepositionMar 20, 2024-
Header (metadata) releaseOct 2, 2024-
Map releaseOct 2, 2024-
UpdateMar 5, 2025-
Current statusMar 5, 2025Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

emd_44171.png

Downloads & links

-
Map

FileDownload / File: emd_44171.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMycolicibacterium smegmatis MmpL5 structure
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 300 pix.
= 321. Å		1.07 Å/pix.
x 300 pix.
= 321. Å		1.07 Å/pix.
x 300 pix.
= 321. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.07 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-0.52785015 - 1.0862187
Average (Standard dev.)-0.00057084113 (±0.021820774)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 321.00003 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: Half Map A

Fileemd_44171_half_map_1.map
AnnotationHalf Map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: Half Map B

Fileemd_44171_half_map_2.map
AnnotationHalf Map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

-
Entire : MmpL5

EntireName: MmpL5
Components
  • Complex: MmpL5
    • Protein or peptide: MmpL5 protein

-
Supramolecule #1: MmpL5

SupramoleculeName: MmpL5 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Mycolicibacterium smegmatis (bacteria)
Molecular weightTheoretical: 105.5 kDa/nm

-
Macromolecule #1: MmpL5 protein

MacromoleculeName: MmpL5 protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mycolicibacterium smegmatis (bacteria)
Molecular weightTheoretical: 106.427109 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MSAPTDDTPT DAIAAPRHSA PPRPRLPWFL RTFAVPIILA WVAVVAILNT VVPTLDEVGE MRAVSMAPND APSTLAIKRV GQVFEEYDT SSSVMIVLEG EEPLGIEAHA FYDKMVADLR ADTEHVQHVQ DFWGDTLTAS GAQSVDGKAA YVQVYIAGDQ G ESLANESV ...String:
MSAPTDDTPT DAIAAPRHSA PPRPRLPWFL RTFAVPIILA WVAVVAILNT VVPTLDEVGE MRAVSMAPND APSTLAIKRV GQVFEEYDT SSSVMIVLEG EEPLGIEAHA FYDKMVADLR ADTEHVQHVQ DFWGDTLTAS GAQSVDGKAA YVQVYIAGDQ G ESLANESV EAVRKIATER ETPSGVKAYV TGAAATSADQ RAEGDASMKL IEGVTFAVIT VMLLAVYRSV ITTLIVLAMV VL GLSGARG IVAFLGFYNV FGLTTFATNM VVTLAIAAAT DYAIFLIGRY QEARRAGEDR ESAYYTMFHG TAHVVLASGL TIA GATLCL HFTRLPYFQT MGVPLAIGML IVVAAALTAG PAVISVVSRF GKTLEPKRFS RSPGWHRVGT ATVRWPGAIL VCAV VAALI GLLALPGYYT TYDDRRYLPD DVPANVGYDA AFRHFSQAKM NPDLMMVETD RDLRNPADFL VIDKIAKALK NVHGI AQVQ TITRPDGDPI EHSTIPYTIG QSGTTQIMNN DYMQTNLDNL LKQADDLQTS IDSMTEMMNI QTELAAVSQS MADKMA QTS DDTADVRDHL ADFDDFFRPI RNYLYWEPHC YDIPMCWSMR SIFESIDGIN TMSDDFQELV PEMRRMADLM PRMVAVM PA QIQSMKNQKQ TLLNQYQVQK AQQDQNMAMQ ENATAMSQAF DAAKNDDSFY LPPEAFETDD FQRGMKLFMS PDGHAVRF T IIHQGDPLTE EGTARMDELK VAAADAIKGT PFEGARIYLG GSAATYNDMQ IGADYDLIIV AASALILIFI IMMVLTRAV VAAAVIVGTV VLSLASAFGL SVLLWQHIVG IPLHWMVLPM SVIVLLAVGA DYNLLLVSRM KEEIHAGIRT GIIRAMVGTG AVVTAAGLV FAFTMASMAV SSLITIGQVG TTIGLGLLFD TLVVRSLMTP SIATLLGRWF WWPQRVRERP VPSKWPTPIQ R TPEEALSH HHHHH

UniProtKB: MmpL5 protein

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration2.0 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4S4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid
100.0 mMNaClsodium chloride
0.005 %C47H88O22Lauryl Maltose Neopentyl Glycol
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 39.4 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Particle selectionNumber selected: 1648768
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 61196
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
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://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