[English] 日本語
Yorodumi
- EMDB-9883: Structure of human soluble guanylate cyclase in the unliganded state -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-9883
TitleStructure of human soluble guanylate cyclase in the unliganded state
Map data
Sample
  • Complex: human soluble guanylate cyclase
    • Protein or peptide: Guanylate cyclase soluble subunit alpha-1
    • Protein or peptide: Guanylate cyclase soluble subunit beta-1
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
Keywordssoluble guanylate cyclase / SIGNALING PROTEIN
Function / homology
Function and homology information


retrograde trans-synaptic signaling by nitric oxide, modulating synaptic transmission / cytidylate cyclase activity / trans-synaptic signaling by nitric oxide, modulating synaptic transmission / guanylate cyclase complex, soluble / guanylate cyclase / cGMP biosynthetic process / guanylate cyclase activity / presynaptic active zone cytoplasmic component / response to oxygen levels / Nitric oxide stimulates guanylate cyclase ...retrograde trans-synaptic signaling by nitric oxide, modulating synaptic transmission / cytidylate cyclase activity / trans-synaptic signaling by nitric oxide, modulating synaptic transmission / guanylate cyclase complex, soluble / guanylate cyclase / cGMP biosynthetic process / guanylate cyclase activity / presynaptic active zone cytoplasmic component / response to oxygen levels / Nitric oxide stimulates guanylate cyclase / relaxation of vascular associated smooth muscle / adenylate cyclase activity / blood circulation / positive regulation of nitric oxide mediated signal transduction / cGMP-mediated signaling / cellular response to nitric oxide / Smooth Muscle Contraction / nitric oxide mediated signal transduction / GABA-ergic synapse / nitric oxide-cGMP-mediated signaling / Hsp90 protein binding / regulation of blood pressure / signaling receptor activity / glutamatergic synapse / heme binding / protein-containing complex binding / GTP binding / metal ion binding / cytosol
Similarity search - Function
Haem NO binding associated / Haem NO binding associated domain superfamily / Heme NO binding associated / Heme NO-binding / H-NOX domain superfamily / Haem-NO-binding / Adenylyl cyclase class-4/guanylyl cyclase, conserved site / Guanylate cyclase signature. / NO signalling/Golgi transport ligand-binding domain superfamily / Adenylyl- / guanylyl cyclase, catalytic domain ...Haem NO binding associated / Haem NO binding associated domain superfamily / Heme NO binding associated / Heme NO-binding / H-NOX domain superfamily / Haem-NO-binding / Adenylyl cyclase class-4/guanylyl cyclase, conserved site / Guanylate cyclase signature. / NO signalling/Golgi transport ligand-binding domain superfamily / Adenylyl- / guanylyl cyclase, catalytic domain / Adenylate and Guanylate cyclase catalytic domain / Adenylyl cyclase class-3/4/guanylyl cyclase / Guanylate cyclase domain profile. / Nucleotide cyclase
Similarity search - Domain/homology
Guanylate cyclase soluble subunit alpha-1 / Guanylate cyclase soluble subunit beta-1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.0 Å
AuthorsChen L / Kang Y
Funding support China, 4 items
OrganizationGrant numberCountry
Ministry of Science and Technology (China)2016YFA0502004 China
National Natural Science Foundation of China31622021 China
National Natural Science Foundation of China31821091 China
National Natural Science Foundation of China31870833 China
CitationJournal: Nature / Year: 2019
Title: Structural insights into the mechanism of human soluble guanylate cyclase.
Authors: Yunlu Kang / Rui Liu / Jing-Xiang Wu / Lei Chen /
Abstract: Soluble guanylate cyclase (sGC) is the primary sensor of nitric oxide. It has a central role in nitric oxide signalling and has been implicated in many essential physiological processes and disease ...Soluble guanylate cyclase (sGC) is the primary sensor of nitric oxide. It has a central role in nitric oxide signalling and has been implicated in many essential physiological processes and disease conditions. The binding of nitric oxide boosts the enzymatic activity of sGC. However, the mechanism by which nitric oxide activates the enzyme is unclear. Here we report the cryo-electron microscopy structures of the human sGCα1β1 heterodimer in different functional states. These structures revealed that the transducer module bridges the nitric oxide sensor module and the catalytic module. Binding of nitric oxide to the β1 haem-nitric oxide and oxygen binding (H-NOX) domain triggers the structural rearrangement of the sensor module and a conformational switch of the transducer module from bending to straightening. The resulting movement of the N termini of the catalytic domains drives structural changes within the catalytic module, which in turn boost the enzymatic activity of sGC.
History
DepositionApr 8, 2019-
Header (metadata) releaseAug 28, 2019-
Map releaseAug 28, 2019-
UpdateMar 27, 2024-
Current statusMar 27, 2024Processing site: PDBj / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.024
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.024
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-6jt0
  • Surface level: 0.024
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_9883.png

Downloads & links

-
Map

FileDownload / File: emd_9883.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 240 pix.
= 250.8 Å		1.05 Å/pix.
x 240 pix.
= 250.8 Å		1.05 Å/pix.
x 240 pix.
= 250.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.045 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.024 / Movie #1: 0.024
Minimum - Maximum-0.046277817 - 0.109003514
Average (Standard dev.)0.00024944055 (±0.0025147407)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 250.79999 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0451.0451.045
M x/y/z240240240
origin x/y/z0.0000.0000.000
length x/y/z250.800250.800250.800
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ132132232
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS240240240
D min/max/mean-0.0460.1090.000

-
Supplemental data

-
Sample components

-
Entire : human soluble guanylate cyclase

EntireName: human soluble guanylate cyclase
Components
  • Complex: human soluble guanylate cyclase
    • Protein or peptide: Guanylate cyclase soluble subunit alpha-1
    • Protein or peptide: Guanylate cyclase soluble subunit beta-1
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE

-
Supramolecule #1: human soluble guanylate cyclase

SupramoleculeName: human soluble guanylate cyclase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

-
Macromolecule #1: Guanylate cyclase soluble subunit alpha-1

MacromoleculeName: Guanylate cyclase soluble subunit alpha-1 / type: protein_or_peptide / ID: 1 / Details: GenBank: AAH28384.1 / Number of copies: 1 / Enantiomer: LEVO / EC number: guanylate cyclase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 77.566484 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MFCTKLKDLK ITGECPFSLL APGQVPNESS EEAAGSSESC KATMPICQDI PEKNIQESLP QRKTSRSRVY LHTLAESICK LIFPEFERL NVALQRTLAK HKIKESRKSL EREDFEKTIA EQAVAAGVPV EVIKESLGEE VFKICYEEDE NILGVVGGTL K DFLNSFST ...String:
MFCTKLKDLK ITGECPFSLL APGQVPNESS EEAAGSSESC KATMPICQDI PEKNIQESLP QRKTSRSRVY LHTLAESICK LIFPEFERL NVALQRTLAK HKIKESRKSL EREDFEKTIA EQAVAAGVPV EVIKESLGEE VFKICYEEDE NILGVVGGTL K DFLNSFST LLKQSSHCQE AGKRGRLEDA SILCLDKEDD FLHVYYFFPK RTTSLILPGI IKAAAHVLYE TEVEVSLMPP CF HNDCSEF VNQPYLLYSV HMKSTKPSLS PSKPQSSLVI PTSLFCKTFP FHFMFDKDMT ILQFGNGIRR LMNRRDFQGK PNF EEYFEI LTPKINQTFS GIMTMLNMQF VVRVRRWDNS VKKSSRVMDL KGQMIYIVES SAILFLGSPC VDRLEDFTGR GLYL SDIPI HNALRDVVLI GEQARAQDGL KKRLGKLKAT LEQAHQALEE EKKKTVDLLC SIFPCEVAQQ LWQGQVVQAK KFSNV TMLF SDIVGFTAIC SQCSPLQVIT MLNALYTRFD QQCGELDVYK VETIGDAYCV AGGLHKESDT HAVQIALMAV KMMELS DEV MSPHGEPIKM RIGLHSGSVF AGVVGVKMPR YCLFGNNVTL ANKFESCSVP RKINVSPTTY RLLKDCPGFV FTPRSRE EL PPNFPSEIPG ICHFLDAYQQ GTNSKPCFQK KDVEDGNANF LGKASGID

UniProtKB: Guanylate cyclase soluble subunit alpha-1

-
Macromolecule #2: Guanylate cyclase soluble subunit beta-1

MacromoleculeName: Guanylate cyclase soluble subunit beta-1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: guanylate cyclase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 70.59932 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD LVAAASKVLN LNAGEILQMF GKMFFVFCQE SGYDTILRV LGSNVREFLQ NLDALHDHLA TIYPGMRAPS FRCTDAEKGK GLILHYYSER EGLQDIVIGI IKTVAQQIHG T EIDMKVIQ ...String:
MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD LVAAASKVLN LNAGEILQMF GKMFFVFCQE SGYDTILRV LGSNVREFLQ NLDALHDHLA TIYPGMRAPS FRCTDAEKGK GLILHYYSER EGLQDIVIGI IKTVAQQIHG T EIDMKVIQ QRNEECDHTQ FLIEEKESKE EDFYEDLDRF EENGTQESRI SPYTFCKAFP FHIIFDRDLV VTQCGNAIYR VL PQLQPGN CSLLSVFSLV RPHIDISFHG ILSHINTVFV LRSKEGLLDV EKLECEDELT GTEISCLRLK GQMIYLPEAD SIL FLCSPS VMNLDDLTRR GLYLSDIPLH DATRDLVLLG EQFREEYKLT QELEILTDRL QLTLRALEDE KKKTDTLLYS VLPP SVANE LRHKRPVPAK RYDNVTILFS GIVGFNAFCS KHASGEGAMK IVNLLNDLYT RFDTLTDSRK NPFVYKVETV GDKYM TVSG LPEPCIHHAR SICHLALDMM EIAGQVQVDG ESVQITIGIH TGEVVTGVIG QRMPRYCLFG NTVNLTSRTE TTGEKG KIN VSEYTYRCLM SPENSDPQFH LEHRGPVSMK GKKEPMQVWF LSRKNTGTEE TKQDDD

UniProtKB: Guanylate cyclase soluble subunit beta-1

-
Macromolecule #3: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 3 / Number of copies: 1 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 229111
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://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