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REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.
by electron microscopy, at 4.00 A resolution
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Entry
Database / IDPORTEIN DATA BANK (PDB) / 2bg9
TitleREFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.
DescriptorACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN, ACETYLCHOLINE RECEPTOR PROTEIN, BETA CHAIN, ACETYLCHOLINE RECEPTOR PROTEIN, DELTA CHAIN, ACETYLCHOLINE RECEPTOR PROTEIN, GAMMA CHAIN
AuthorsUnwin, N.
Images
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KeywordsION CHANNEL/RECEPTOR, ION CHANNEL/RECEPTOR, ACETYLCHOLINE RECEPTOR, ION CHANNEL, ELECTRON MICROSCOPY, ION TRANSPORT, POSTSYNAPTIC MEMBRANE,
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Deposition2004-12-17
Release2005-02-16
PDBj Mine pagesSummaryStructural DetailsExperimental DetailsFunctional Details
Other databasesRCSB-PDBPDBeCATHCEFSSPSCOPVAST
Article
Citation - primary
ArticleJ. Mol. Biol., Vol. 346, Issue 4, Page 967-89, Year 2005
TitleRefined structure of the nicotinic acetylcholine receptor at 4A resolution.
AuthorsNigel Unwin
AffiliationMRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
ChemicalsProtein Subunits, Receptors, Nicotinic
KeywordsAmino Acid Sequence, Animals, Binding Sites, Crystallography, X-Ray, Ion Channel Gating, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Folding, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits, Receptors, Nicotinic, Sequence Alignment, Static Electricity, Torpedo
LinksPubMed: 15701510 DOI: 10.1016/j.jmb.2004.12.031
Citation - 1
ArticleNature, Vol. 423, Issue 6943, Page 949-55, Year 2003
TitleStructure and gating mechanism of the acetylcholine receptor pore.
AuthorsAtsuo Miyazawa, Yoshinori Fujiyoshi, Nigel Unwin
AffiliationRIKEN Harima Institute, 1-1-1 Kouto, Mikazuki-cho, Sayo, Hyogo 679-5148, Japan.
ChemicalsIons, Receptors, Cholinergic, Acetylcholine (51-84-3)
KeywordsAcetylcholine, Amino Acid Sequence, Animals, Crystallization, Electric Conductivity, Ion Channel Gating, Ions, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Folding, Receptors, Cholinergic, Torpedo
LinksPubMed: 12827192 DOI: 10.1038/nature01748
Components
ID 1 : NICOTINIC ACETYLCHOLINE RECEPTOR
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DescriptionACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN
Typepolypeptide(L)
Formula weight42501.766 Da
Number of molecules2.
SequenceSEHETRLVAN LLENYNKVIR PVEHHTHFVD ITVGLQLIQL INVDEVNQIV ETNVRLRQQW IDVRLRWNPA DYGGIKKIRL PSDDVWLPDL VLYNNADGDF AIVHMTKLLL DYTGKIMWTP PAIFKSYCEI IVTHFPFDQQ NCTMKLGIWT YDGTKVSISP ESDRPDLSTF MESGEWVMKD YRGWKHWVYY TCCPDTPYLD ITYHFIMQRI PLYFVVNVII PCLLFSFLTV LVFYLPTDSG EKMTLSISVL LSLTVFLLVI VELIPSTSSA VPLIGKYMLF TMIFVISSII VTVVVINTHH RSPSTHSAIE GVKYIAEHMK SDEESSNAAE EWKYVAMVID HILLCVFMLI CIIGTVSVFA GRLIELSQEG
SourceMethod: Isolated from a natural source
Common name: MARBLED ELECTRIC RAY
NCBI_taxonomy: ID:7788
Organ: ELECTRIC ORGAN
Organism scientific: TORPEDO MARMORATA
Tissue: DERIVED FROM MUSCLE
LinksUniProt: ACHA_TORMA
ID 2 : NICOTINIC ACETYLCHOLINE RECEPTOR
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DescriptionACETYLCHOLINE RECEPTOR PROTEIN, BETA CHAIN
Typepolypeptide(L)
Formula weight42167.836 Da
Number of molecules1.
SequenceSVMEDTLLSV LFENYNPKVR PSQTVGDKVT VRVGLTLTSL LILNEKNEEM TTSVFLNLAW TDYRLQWDPA AYEGIKDLSI PSDDVWQPDI VLMNNNDGSF EITLHVNVLV QHTGAVSWHP SAIYRSSCTI KVMYFPFDWQ NCTMVFKSYT YDTSEVILQH ALDAMINQDA FTENGQWSIE HKPSRKNWRS DDPSYEDVTF YLIIQRKPLF YIVYTIVPCI LISILAILVF YLPPDAGEKM SLSISALLAL TVFLLLLADK VPETSLSVPI IISYLMFIMI LVAFSVILSV VVLNLHHRSP NTHEAVEAIK YIAEQLESAS EFDDLKKDWQ YVAMVADRLF LYIFITMCSI GTFSIFLDAS HNVPPDNPFA
SourceMethod: Isolated from a natural source
Common name: MARBLED ELECTRIC RAY
NCBI_taxonomy: ID:7788
Organ: ELECTRIC ORGAN
Organism scientific: TORPEDO MARMORATA
Tissue: DERIVED FROM MUSCLE
LinksUniProt: Q6S3I0
ID 3 : NICOTINIC ACETYLCHOLINE RECEPTOR
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DescriptionACETYLCHOLINE RECEPTOR PROTEIN, DELTA CHAIN
Typepolypeptide(L)
Formula weight42281.164 Da
Number of molecules1.
SequenceVNEEERLIND LLIVNKYNKH VRPVKHNNEV VNIALSLTLS NLISLKETDE TLTTNVWMDH AWYDHRLTWN ASEYSDISIL RLRPELIWIP DIVLQNNNDG QYNVAYFCNV LVRPNGYVTW LPPAIFRSSC PINVLYFPFD WQNCSLKFTA LNYNANEISM DLIIDPEAFT ENGEWEIIHK PAKKNIYGDK FPNGTNYQDV TFYLIIRRKP LFYVINFITP CVLISFLAAL AFYLPAESGE KMSTAICVLL AQAVFLLLTS QRLPETALAV PLIGKYLMFI MSLVTGVVVN CGIVLNFHFR TPSTHSGIDS TNYIVKQIKE KNAYDEEVGN WNLVGQTIDR LSMFIITPVM VLGTIFIFVM GNFNRPPAK
SourceMethod: Isolated from a natural source
Common name: MARBLED ELECTRIC RAY
NCBI_taxonomy: ID:7788
Organ: ELECTRIC ORGAN
Organism scientific: TORPEDO MARMORATA
Tissue: DERIVED FROM MUSCLE
LinksUniProt: Q6S3H8
ID 4 : NICOTINIC ACETYLCHOLINE RECEPTOR
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DescriptionACETYLCHOLINE RECEPTOR PROTEIN, GAMMA CHAIN
Typepolypeptide(L)
Formula weight42299.988 Da
Number of molecules1.
SequenceNEEGRLIEKL LGDYDKRIKP AKTLDHVIDV TLKLTLTNLI SLNEKEEALT TNVWIEIQWN DYRLSWNTSE YEGIDLVRIP SELLWLPDVV LENNVDGQFE VAYYANVLVY NDGSMYWLPP AIYRSTCPIA VTYFPFDWQN CSLVFRSQTY NAHEVNLQLS AEEGIDPEDF TENGEWTIRH RPAKKNYNWQ LTKDDIDFQE IIFFLIIQRK PLFYIINIIA PCVLISSLVV LVYFLPAQAG GQKCTLSISV LLAQTIFLFL IAQKVPETSL NVPLIGKYLI FVMFVSLVIV TNCVIVLNVS LRTPNTHSCV EACNFIAKST KEQNDSGSEN ENWVLIGKVI DKACFWIALL LFSLGTLAIF LTGHLNQVPE
SourceMethod: Isolated from a natural source
Common name: MARBLED ELECTRIC RAY
Details: INHABITS THE EUROPEAN COAST
NCBI_taxonomy: ID:7788
Organ: ELECTRIC ORGAN
Organism scientific: TORPEDO MARMORATA
Tissue: DERIVED FROM MUSCLE
LinksUniProt: Q6S3H9
Sample
Assembly
NamePOSTSYNAPTIC MEMBRANE
Buffer
Name100MM SODIUM CACODYLATE
Experiment
Reconstruction methodHELICAL
Specimen typeVITREOUS ICE (CRYO EM)
Sample preparation
pH6.8
Sample support
DetailsHOLEY CARBON
Vitrification
DetailsLIQUID ETHANE
Assembly
Method detailsPQS
Oligomeric count5
Oligomeric detailspentameric
Electron Microscopy
Imaging
Accelerating voltage300 kV
Calibrated magnification36800 X
Date2000-10-01
DetailsTHE SPECIMENS WERE TUBULAR CRYSTALS GROWN IN LOW SALT BUFFER FROM ISOLATED TORPEDO POSTSYNAPTIC MEMBRANES. THEY WERE APPLIED TO THE MICROSCOPE GRIDS AND FROZEN IN THE SAME SOLUTION. THESE CRYSTALS WERE TOO SMALL AND DISTORTED TO YIELD MEANINGFUL ELECTRON DIFFRACTION PATTERNS, SO BOTH THE AMPLITUDE AND THE PHASE TERMS HAD TO BE MEASURED FROM FOURIER TRANSFORMS OF THE IMAGES. THE IMAGES WERE RECORDED USING A DOSE OF 2000 ELECTRONS/NM2 DURING THE PERIOD: JAN-1996 TO OCT-2002. THE DATASETS INVOLVED 4 HELICAL FAMILIES OF TUBES. STRUCTURES WERE SYNTHESISED FROM THE AMPLITUDE AND PHASE TERMS DERIVED FROM EACH FAMILY. THE FINAL DATASET WAS OBTAINED BY AVERAGING THESE 4 STRUCTURES IN REAL SPACE.
Electron sourceFIELD EMISSION GUN
Illumination modeBRIGHT FIELD
Microscope modelJEM300SFF
ModeLOW DOSE
Nominal Cs1.3 mm
Nominal defocus max1800. nm
Nominal defocus min800. nm
Nominal magnification40000 X
Temperature4.2 Kelvin
Detector
TypeSO-163 FILM
Image scans
Number digital images342
Processing
Refine
Ls d res high4.00 A
Refine hist
D res high4.00
Solvent atoms0
Total atoms14924
Ligand atoms0
Nucleic acid atoms0
Protein atoms14924
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