[English] 日本語
Yorodumi
- EMDB-42452: Pfr state of Stigmatella aurantiaca bacteriophytochrome 2 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-42452
TitlePfr state of Stigmatella aurantiaca bacteriophytochrome 2
Map dataPr state of Stigmatella aurantiaca bacteriophytochrome 2
Sample
  • Organelle or cellular component: Stigmatella aurantiaca bacteriophytochrome
    • Protein or peptide: Bacteriophytochrome (Light-regulated signal transduction histidine kinase)
  • Ligand: BILIVERDINE IX ALPHA
KeywordsRed light photoreceptor / two component system / SIGNALING PROTEIN
Function / homology
Function and homology information


detection of visible light / histidine kinase / phosphorelay sensor kinase activity / photoreceptor activity / regulation of DNA-templated transcription
Similarity search - Function
: / Phytochrome / Phytochrome, PHY domain superfamily / PAS fold-2 / PAS fold / Phytochrome, central region / Phytochrome region / Phytochrome chromophore attachment domain / Phytochrome chromophore attachment site domain profile. / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain ...: / Phytochrome / Phytochrome, PHY domain superfamily / PAS fold-2 / PAS fold / Phytochrome, central region / Phytochrome region / Phytochrome chromophore attachment domain / Phytochrome chromophore attachment site domain profile. / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily / Histidine kinase domain / Histidine kinase domain profile. / GAF domain / Domain present in phytochromes and cGMP-specific phosphodiesterases. / GAF domain / GAF-like domain superfamily / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / PAS domain superfamily / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily
Similarity search - Domain/homology
Biological speciesStigmatella aurantiaca (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.75 Å
AuthorsMalla TN / Schmidt M / Stojkovic EA
Funding support United States, 2 items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)NSF-STC-1231306 United States
National Science Foundation (NSF, United States)NSF STC BioXFEL center award 6227 United States
CitationJournal: Sci Adv / Year: 2024
Title: Photoreception and signaling in bacterial phytochrome revealed by single-particle cryo-EM.
Authors: Tek Narsingh Malla / Carolina Hernandez / Srinivasan Muniyappan / David Menendez / Dorina Bizhga / Joshua H Mendez / Peter Schwander / Emina A Stojković / Marius Schmidt /
Abstract: Phytochromes are red-light photoreceptors discovered in plants with homologs in bacteria and fungi that regulate a variety of physiological responses. They display a reversible photocycle between two ...Phytochromes are red-light photoreceptors discovered in plants with homologs in bacteria and fungi that regulate a variety of physiological responses. They display a reversible photocycle between two distinct states: a red-light-absorbing Pr state and a far-red light-absorbing Pfr state. The photoconversion regulates the activity of an enzymatic domain, usually a histidine kinase (HK). The molecular mechanism that explains how light controls the HK activity is not understood because structures of unmodified bacterial phytochromes with HK activity are missing. Here, we report three cryo-electron microscopy structures of a wild-type bacterial phytochrome with HK activity determined as Pr and Pfr homodimers and as a Pr/Pfr heterodimer with individual subunits in distinct states. We propose that the Pr/Pfr heterodimer is a physiologically relevant signal transduction intermediate. Our results offer insight into the molecular mechanism that controls the enzymatic activity of the HK as part of a bacterial two-component system that perceives and transduces light signals.
History
DepositionOct 23, 2023-
Header (metadata) releaseSep 25, 2024-
Map releaseSep 25, 2024-
UpdateSep 25, 2024-
Current statusSep 25, 2024Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_42452.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPr state of Stigmatella aurantiaca bacteriophytochrome 2
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 400 pix.
= 337.6 Å
0.84 Å/pix.
x 400 pix.
= 337.6 Å
0.84 Å/pix.
x 400 pix.
= 337.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.844 Å
Density
Contour LevelBy AUTHOR: 0.032
Minimum - Maximum-0.15740578 - 0.32832897
Average (Standard dev.)-0.00010902606 (±0.0071018743)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 337.6 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Sample components

-
Entire : Stigmatella aurantiaca bacteriophytochrome

EntireName: Stigmatella aurantiaca bacteriophytochrome
Components
  • Organelle or cellular component: Stigmatella aurantiaca bacteriophytochrome
    • Protein or peptide: Bacteriophytochrome (Light-regulated signal transduction histidine kinase)
  • Ligand: BILIVERDINE IX ALPHA

-
Supramolecule #1: Stigmatella aurantiaca bacteriophytochrome

SupramoleculeName: Stigmatella aurantiaca bacteriophytochrome / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Stigmatella aurantiaca (bacteria)

-
Macromolecule #1: Bacteriophytochrome (Light-regulated signal transduction histidin...

MacromoleculeName: Bacteriophytochrome (Light-regulated signal transduction histidine kinase)
type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Stigmatella aurantiaca (bacteria)
Molecular weightTheoretical: 81.150758 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MRPSVSELEL SQCDREPIHL LGGIQAYGVL LAFRGPDRRL EVVSANTQAL LGRPPEALLG KTAAQVLPAE LWAQWELLSA RGALRVALP SGPYRALLHE SDGLTVLELE PAELQPDMEE TALELVRRLV SPLAGAKGTR ELLQTAANTV RALTGFDRVM V YRFDADWH ...String:
MRPSVSELEL SQCDREPIHL LGGIQAYGVL LAFRGPDRRL EVVSANTQAL LGRPPEALLG KTAAQVLPAE LWAQWELLSA RGALRVALP SGPYRALLHE SDGLTVLELE PAELQPDMEE TALELVRRLV SPLAGAKGTR ELLQTAANTV RALTGFDRVM V YRFDADWH GEVLAESKRE GMDGFLGMHF PATDIPVQAR ALYTRNPLRL IANARARPVP LVPSVVPELG RPLDLSGSAL RS VSPIHLE YLRNMGVEAS FSLSLLKDGA LWGLIACHHL APLHLSYERR RACEVLTQLL ALQLSSEERA AEAAEDSHRA ALL GPLATS LGAGGTLEEA LAKDGARVLE LTGATGAALL LGGEPLLVGR TPSMDEVEAL AAWLAPQPFQ TSFHTERLGS LYPP LAARA DVAAGLLAVR LAPASSRLAL WFRPEAVRTI SWAGNPRKPA EPEPGHARLH PRGSFQAWEE TVRETSPAWK RADLA AAEG FRSALIGVVL RQAAELERLS EALSRSNAEL DAFGHTVAHD LKEPLRGIQQ YAGFVMEDYH GALGPEGRGH MESLMW LAQ RSGDMLDGLF EYSRAGRVDL AWGEVNMQEV VDEVLATLST RFQAEKLTVR MPRRLPTVRC DGIRIAQVWA NLLVNAA KY QEGPERWVEA GFHGPGEPRP GAAGRYASAY VFYVKDPGIG IAPPFHEAIF EMFRRLHSAK AYGGGTGVGL AIARRLVQ L HGGALWVDSA PKQGATFYFT LGRGPG

UniProtKB: histidine kinase

-
Macromolecule #2: BILIVERDINE IX ALPHA

MacromoleculeName: BILIVERDINE IX ALPHA / type: ligand / ID: 2 / Number of copies: 2 / Formula: BLA
Molecular weightTheoretical: 582.646 Da
Chemical component information

ChemComp-BLA:
BILIVERDINE IX ALPHA

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 59.31 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.75 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 155342
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
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