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- EMDB-41411: Structural architecture of the acidic region of the B domain of c... -

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Basic information

Entry
Database: EMDB / ID: EMD-41411
TitleStructural architecture of the acidic region of the B domain of coagulation factor V
Map dataCoagulation plasma factor V - Sharpened composite map
Sample
  • Tissue: Coagulation plasma Factor V
    • Protein or peptide: Coagulation factor V
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
KeywordsCoagulation / Pro-cofactor / Factor V / B Domain / Acidic Region / BLOOD CLOTTING
Function / homology
Function and homology information


response to vitamin K / platelet alpha granule / Cargo concentration in the ER / COPII-coated ER to Golgi transport vesicle / COPII-mediated vesicle transport / blood circulation / Common Pathway of Fibrin Clot Formation / endoplasmic reticulum-Golgi intermediate compartment membrane / platelet alpha granule lumen / Post-translational protein phosphorylation ...response to vitamin K / platelet alpha granule / Cargo concentration in the ER / COPII-coated ER to Golgi transport vesicle / COPII-mediated vesicle transport / blood circulation / Common Pathway of Fibrin Clot Formation / endoplasmic reticulum-Golgi intermediate compartment membrane / platelet alpha granule lumen / Post-translational protein phosphorylation / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / blood coagulation / Platelet degranulation / extracellular vesicle / endoplasmic reticulum lumen / copper ion binding / extracellular space / extracellular region / membrane / plasma membrane
Similarity search - Function
Coagulation factor 5/8-like / : / Coagulation factors 5/8 type C domain (FA58C) signature 2. / Multicopper oxidases, conserved site / Multicopper oxidases signature 1. / Coagulation factors 5/8 type C domain (FA58C) signature 1. / Coagulation factor 5/8 C-terminal domain, discoidin domain / Coagulation factors 5/8 type C domain (FA58C) profile. / F5/8 type C domain / Coagulation factor 5/8 C-terminal domain ...Coagulation factor 5/8-like / : / Coagulation factors 5/8 type C domain (FA58C) signature 2. / Multicopper oxidases, conserved site / Multicopper oxidases signature 1. / Coagulation factors 5/8 type C domain (FA58C) signature 1. / Coagulation factor 5/8 C-terminal domain, discoidin domain / Coagulation factors 5/8 type C domain (FA58C) profile. / F5/8 type C domain / Coagulation factor 5/8 C-terminal domain / Multicopper oxidase, N-terminal / Multicopper oxidase / Cupredoxin / Galactose-binding-like domain superfamily
Similarity search - Domain/homology
Coagulation factor V
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.05 Å
AuthorsMohammed BM / Basore K / Summers B / Pelc LA / Di Cera E
Funding support United States, 5 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)HL049413, HL139554 and HL147821 United States
Childrens Discovery Institute of Washington University and St. Louis Childrens HospitalCDI-CORE-2015-505 and CDI-CORE-2019-813 United States
The Foundation for Barnes-Jewish Hospital3770 United States
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)DK020579 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)CA091842 United States
CitationJournal: J.Thromb.Haemost. / Year: 2024
Title: Structural architecture of the acidic region of the B domain of coagulation factor V.
Authors: Mohammed BM / Basore K / Summers B / Pelc LA / Di Cera E
History
DepositionAug 1, 2023-
Header (metadata) releaseOct 4, 2023-
Map releaseOct 4, 2023-
UpdateNov 20, 2024-
Current statusNov 20, 2024Processing site: RCSB / Status: Released

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Structure visualization

Downloads & links

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Map

FileDownload / File: emd_41411.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCoagulation plasma factor V - Sharpened composite map
Voxel sizeX=Y=Z: 1.1 Å
Density
Contour LevelBy AUTHOR: 2.65
Minimum - Maximum-30.495039999999999 - 62.987549999999999
Average (Standard dev.)-0.000000000002527 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 281.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Coagulation plasma Factor V

EntireName: Coagulation plasma Factor V
Components
  • Tissue: Coagulation plasma Factor V
    • Protein or peptide: Coagulation factor V
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

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Supramolecule #1: Coagulation plasma Factor V

SupramoleculeName: Coagulation plasma Factor V / type: tissue / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human) / Tissue: Blood

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Macromolecule #1: Coagulation factor V

MacromoleculeName: Coagulation factor V / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 248.973234 KDa
SequenceString: AQLRQFYVAA QGISWSYRPE PTNSSLNLSV TSFKKIVYRE YEPYFKKEKP QSTISGLLGP TLYAEVGDII KVHFKNKADK PLSIHPQGI RYSKLSEGAS YLDHTFPAEK MDDAVAPGRE YTYEWSISED SGPTHDDPPC LTHIYYSHEN LIEDFNSGLI G PLLICKKG ...String:
AQLRQFYVAA QGISWSYRPE PTNSSLNLSV TSFKKIVYRE YEPYFKKEKP QSTISGLLGP TLYAEVGDII KVHFKNKADK PLSIHPQGI RYSKLSEGAS YLDHTFPAEK MDDAVAPGRE YTYEWSISED SGPTHDDPPC LTHIYYSHEN LIEDFNSGLI G PLLICKKG TLTEGGTQKT FDKQIVLLFA VFDESKSWSQ SSSLMYTVNG YVNGTMPDIT VCAHDHISWH LLGMSSGPEL FS IHFNGQV LEQNHHKVSA ITLVSATSTT ANMTVGPEGK WIISSLTPKH LQAGMQAYID IKNCPKKTRN LKKITREQRR HMK RWEYFI AAEEVIWDYA PVIPANMDKK YRSQHLDNFS NQIGKHYKKV MYTQYEDESF TKHTVNPNMK EDGILGPIIR AQVR DTLKI VFKNMASRPY SIYPHGVTFS PYEDEVNSSF TSGRNNTMIR AVQPGETYTY KWNILEFDEP TENDAQCLTR PYYSD VDIM RDIASGLIGL LLICKSRSLD RRGIQRAADI EQQAVFAVFD ENKSWYLEDN INKFCENPDE VKRDDPKFYE SNIMST ING YVPESITTLG FCFDDTVQWH FCSVGTQNEI LTIHFTGHSF IYGKRHEDTL TLFPMRGESV TVTMDNVGTW MLTSMNS SP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE STVMATRKMH DRLEPEDEES DADYDYQNRL AAALGIRSFR NSSLNQEE E EFNLTALALE NGTEFVSSNT DIIVGSNYSS PSNISKFTVN NLAEPQKAPS HQQATTAGSP LRHLIGKNSV LNSSTAEHS SPYSEDPIED PLQPDVTGIR LLSLGAGEFK SQEHAKHKGP KVERDQAAKH RFSWMKLLAH KVGRHLSQDT GSPSGMRPWE DLPSQDTGS PSRMRPWKDP PSDLLLLKQS NSSKILVGRW HLASEKGSYE IIQDTDEDTA VNNWLISPQN ASRAWGESTP L ANKPGKQS GHPKFPRVRH KSLQVRQDGG KSRLKKSQFL IKTRKKKKEK HTHHAPLSPR TFHPLRSEAY NTFSERRLKH SL VLHKSNE TSLPTDLNQT LPSMDFGWIA SLPDHNQNSS NDTGQASCPP GLYQTVPPEE HYQTFPIQDP DQMHSTSDPS HRS SSPELS EMLEYDRSHK SFPTDISQMS PSSEHEVWQT VISPDLSQVT LSPELSQTNL SPDLSHTTLS PELIQRNLSP ALGQ MPISP DLSHTTLSPD LSHTTLSLDL SQTNLSPELS QTNLSPALGQ MPLSPDLSHT TLSLDFSQTN LSPELSHMTL SPELS QTNL SPALGQMPIS PDLSHTTLSL DFSQTNLSPE LSQTNLSPAL GQMPLSPDPS HTTLSLDLSQ TNLSPELSQT NLSPDL SEM PLFADLSQIP LTPDLDQMTL SPDLGETDLS PNFGQMSLSP DLSQVTLSPD ISDTTLLPDL SQISPPPDLD QIFYPSE SS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDD P YKTDVRTNIN SSRDPDNIAA WYLRSNNGNR RNYYIAAEEI SWDYSEFVQR ETDIEDSDDI PEDTTYKKVV FRKYLDSTF TKRDPRGEYE EHLGILGPII RAEVDDVIQV RFKNLASRPY SLHAHGLSYE KSSEGKTYED DSPEWFKEDN AVQPNSSYTY VWHATERSG PESPGSACRA WAYYSAVNPE KDIHSGLIGP LLICQKGILH KDSNMPMDMR EFVLLFMTFD EKKSWYYEKK S RSSWRLTS SEMKKSHEFH AINGMIYSLP GLKMYEQEWV RLHLLNIGGS QDIHVVHFHG QTLLENGNKQ HQLGVWPLLP GS FKTLEMK ASKPGWWLLN TEVGENQRAG MQTPFLIMDR DCRMPMGLST GIISDSQIKA SEFLGYWEPR LARLNNGGSY NAW SVEKLA AEFASKPWIQ VDMQKEVIIT GIQTQGAKHY LKSCYTTEFY VAYSSNQINW QIFKGNSTRN VMYFNGNSDA STIK ENQFD PPIVARYIRI SPTRAYNRPT LRLELQGCEV NGCSTPLGME NGKIENKQIT ASSFKKSWWG DYWEPFRARL NAQGR VNAW QAKANNNKQW LEIDLLKIKK ITAIITQGCK SLSSEMYVKS YTIHYSEQGV EWKPYRLKSS MVDKIFEGNT NTKGHV KNF FNPPIISRFI RVIPKTWNQS IALRLELFGC DIY

UniProtKB: Coagulation factor V

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Macromolecule #2: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 2 / Number of copies: 4 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.2 mg/mL
BufferpH: 7.4 / Details: 20 mM HEPES, 150 mM NaCl, 5 mM CaCl2
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: OTHER / Pretreatment - Pressure: 0.009300000000000001 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV
Details0.1 and 0.2 mg/mL

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Electron microscopy

MicroscopeFEI TITAN
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 4000 pixel / Digitization - Dimensions - Height: 4000 pixel / Number grids imaged: 2 / Number real images: 8429 / Average exposure time: 1.65 sec. / Average electron dose: 66.0 e/Å2
Details: 2 Grids imaged one at 0.1 mg/mL and the second at 0.2 mg/mL using the same acquisition parameters.
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 0.01 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN

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Image processing

Particle selectionNumber selected: 1257129
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Algorithm: BACK PROJECTION / Resolution.type: BY AUTHOR / Resolution: 3.05 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.2.1) / Number images used: 680564
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE

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