[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleMolecular insights into capsular polysaccharide secretion.
Journal, issue, pagesNature, Vol. 628, Issue 8009, Page 901-909, Year 2024
Publish dateApr 3, 2024
AuthorsJeremi Kuklewicz / Jochen Zimmer /
PubMed AbstractCapsular polysaccharides (CPSs) fortify the cell boundaries of many commensal and pathogenic bacteria. Through the ABC-transporter-dependent biosynthesis pathway, CPSs are synthesized intracellularly ...Capsular polysaccharides (CPSs) fortify the cell boundaries of many commensal and pathogenic bacteria. Through the ABC-transporter-dependent biosynthesis pathway, CPSs are synthesized intracellularly on a lipid anchor and secreted across the cell envelope by the KpsMT ABC transporter associated with the KpsE and KpsD subunits. Here we use structural and functional studies to uncover crucial steps of CPS secretion in Gram-negative bacteria. We show that KpsMT has broad substrate specificity and is sufficient for the translocation of CPSs across the inner bacterial membrane, and we determine the cell surface organization and localization of CPSs using super-resolution fluorescence microscopy. Cryo-electron microscopy analyses of the KpsMT-KpsE complex in six different states reveal a KpsE-encaged ABC transporter, rigid-body conformational rearrangements of KpsMT during ATP hydrolysis and recognition of a glycolipid inside a membrane-exposed electropositive canyon. In vivo CPS secretion assays underscore the functional importance of canyon-lining basic residues. Combined, our analyses suggest a molecular model of CPS secretion by ABC transporters.
External linksNature / PubMed:38570679 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 4.4 Å
Structure data

EMDB-41592, PDB-8tsh:
S. thermodepolymerans KpsMT(E151Q)-KpsE in complex with ATP
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-41593, PDB-8tsi:
S. thermodepolymerans KpsMT-KpsE in complex with ADP:AlF4-
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-41595, PDB-8tsl:
S. thermodepolymerans KpsM-KpsE in Apo 2 state with rigid body fitted KpsT
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-41601, PDB-8tsw:
S. thermodepolymerans KpsMT-KpsE Apo 1
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-41602, PDB-8tt3:
S. thermodepolymerans KpsM-KpsE in Glycolipid 2 state with rigid body fitted KpsT
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-41626, PDB-8tun:
S. thermodepolymerans KpsM-KpsE in Glycolipid 1 state with rigid body fitted KpsT
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-41677: S. thermodepolymerans KpsMT-KpsE Apo 1 - consensus map
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-41678: S. thermodepolymerans KpsMT-KpsE Apo 1 - KpsT-focused map
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-41681: S. thermodepolymerans KpsMT(E151Q)-KpsE in complex with ATP - consensus map
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-41682: S. thermodepolymerans KpsMT(E151Q)-KpsE in complex with ATP - crown focused map
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-41697: S. thermodepolymerans KpsMT-KpsE in Apo 2 state - consensus map
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-41698: S. thermodepolymerans KpsMT-KpsE in Apo 2 state - KpsT focused map
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-41718: S. thermodepolymerans KpsMT-KpsE with bound glycolipid - state 1 - consensus map
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-41720: S. thermodepolymerans KpsMT-KpsE with bound glycolipid - state 1 - KpsT focused map
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-41721: S. thermodepolymerans KpsMT-KpsE with bound glycolipid - state 1 - KpsM focused map
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-41771: S. thermodepolymerans KpsMT-KpsE with bound glycolipid - state 2 - consensus map
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-41772: S. thermodepolymerans KpsMT-KpsE with bound glycolipid - state 2 - KpsT focused map
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-41773: S. thermodepolymerans KpsMT-KpsE with bound glycolipid - state 2 - KpsM focused map
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-ALF:
TETRAFLUOROALUMINATE ION


ChemComp, No image

ChemComp-KJ9:
Unknown entry

Source
  • caldimonas thermodepolymerans (bacteria)
KeywordsMEMBRANE PROTEIN / ABC transporter / Capsular polysaccharide

+
About Yorodumi Papers

-
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 Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more