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- PDB-1h8b: EF-hands 3,4 from alpha-actinin / Z-repeat 7 from titin -

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Basic information

Entry
Database: PDB / ID: 1h8b
TitleEF-hands 3,4 from alpha-actinin / Z-repeat 7 from titin
Components
  • ALPHA-ACTININ 2, SKELETAL MUSCLE ISOFORM
  • TITIN
KeywordsSTRUCTURAL PROTEIN / Z-DISK STRUCTURAL COMPLEX
Function / homology
Function and homology information


actin filament uncapping / FATZ binding / titin Z domain binding / phospholipase C-activating angiotensin-activated signaling pathway / positive regulation of endocytic recycling / positive regulation of potassium ion transmembrane transporter activity / negative regulation of potassium ion transmembrane transporter activity / telethonin binding / positive regulation of cation channel activity / LIM domain binding ...actin filament uncapping / FATZ binding / titin Z domain binding / phospholipase C-activating angiotensin-activated signaling pathway / positive regulation of endocytic recycling / positive regulation of potassium ion transmembrane transporter activity / negative regulation of potassium ion transmembrane transporter activity / telethonin binding / positive regulation of cation channel activity / LIM domain binding / negative regulation of protein localization to cell surface / microspike assembly / postsynaptic actin cytoskeleton / muscle cell development / positive regulation of potassium ion transport / focal adhesion assembly / Assembly and cell surface presentation of NMDA receptors / Striated Muscle Contraction / cardiac muscle cell development / Nephrin family interactions / sarcomere organization / structural constituent of muscle / cortical actin cytoskeleton / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / pseudopodium / postsynaptic density, intracellular component / negative regulation of potassium ion transport / Long-term potentiation / titin binding / phosphatidylinositol-4,5-bisphosphate binding / regulation of membrane potential / Ras activation upon Ca2+ influx through NMDA receptor / cytoskeletal protein binding / nuclear receptor coactivator activity / platelet alpha granule lumen / filopodium / cell projection / actin filament / protein localization to plasma membrane / postsynaptic density membrane / Z disc / actin filament binding / integrin binding / Platelet degranulation / cell junction / actin binding / actin cytoskeleton organization / RAF/MAP kinase cascade / regulation of apoptotic process / transmembrane transporter binding / dendritic spine / cytoskeleton / cell adhesion / protein domain specific binding / focal adhesion / glutamatergic synapse / calcium ion binding / extracellular exosome / extracellular region / identical protein binding / cytosol
Similarity search - Function
Titin, Z repeat / Titin Z / EF-hand, Ca insensitive / Ca2+ insensitive EF hand / Ca2+ insensitive EF hand / Spectrin repeat / Spectrin repeat / Spectrin/alpha-actinin / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. ...Titin, Z repeat / Titin Z / EF-hand, Ca insensitive / Ca2+ insensitive EF hand / Ca2+ insensitive EF hand / Spectrin repeat / Spectrin repeat / Spectrin/alpha-actinin / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Spectrin repeats / Actinin-type actin-binding domain, conserved site / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Immunoglobulin I-set / Immunoglobulin I-set domain / EF-hand / Recoverin; domain 1 / EF-hand domain pair / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / EF-hand, calcium binding motif / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Titin / Alpha-actinin-2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
ORYCTOLAGUS CUNICULUS (rabbit)
MethodSOLUTION NMR / TORSION ANGLE DYNAMICS, CARTESIAN DYANMICS
AuthorsAtkinson, R.A. / Joseph, C. / Kelly, G. / Muskett, F.W. / Frenkiel, T.A. / Nietlispach, D. / Pastore, A.
Citation
Journal: Nat.Struct.Biol. / Year: 2001
Title: Ca2+-Independent Binding of an EF-Hand Domain to a Novel Motif in the Alpha-Actinin-Titin Complex
Authors: Atkinson, R.A. / Joseph, C. / Kelly, G. / Muskett, F.W. / Frenkiel, T.A. / Nietlispach, D. / Pastore, A.
#1: Journal: Biochemistry / Year: 2000
Title: The Binding of Alpha-Actinin to Titin: Implications for Z-Disk Assembly
Authors: Atkinson, R.A. / Joseph, C. / Piaz, F.D. / Birolo, L. / Stier, G. / Pucci, P. / Pastore, A.
History
DepositionFeb 1, 2001Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 30, 2001Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr
Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED.
Remark 700 SHEET DETERMINATION METHOD: AUTHOR PROVIDED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ALPHA-ACTININ 2, SKELETAL MUSCLE ISOFORM
B: TITIN


Theoretical massNumber of molelcules
Total (without water)13,7442
Polymers13,7442
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)30 / 50LOWEST ENERGIES
RepresentativeModel #1

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Components

#1: Protein ALPHA-ACTININ 2, SKELETAL MUSCLE ISOFORM / ACT-EF34


Mass: 8077.011 Da / Num. of mol.: 1 / Fragment: EF-HANDS 3&4 RESIDUE 822-894
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: MUSCLESkeletal muscle / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P35609
#2: Protein TITIN / / ZR7


Mass: 5667.321 Da / Num. of mol.: 1 / Fragment: Z-REPEAT 7 RESIDUES 648-698
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ORYCTOLAGUS CUNICULUS (rabbit) / Tissue: MUSCLESkeletal muscle / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: O97791
Compound detailsCHAIN A ENGINEERED MUTATION THR822MET, MODIFIED FOR EXPRESSION F-ACTIN CROSS-LINKING PROTEIN IS ...CHAIN A ENGINEERED MUTATION THR822MET, MODIFIED FOR EXPRESSION F-ACTIN CROSS-LINKING PROTEIN IS INVOLVED IN ANCHORING OF ACTIN TO A VARIETY OF INTRACELLULAR STRUCTURES.

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: SEE PUBLICATION
NMR detailsText: THE STRUCTURE OF THE COMPLEX WAS DETERMINED USING CONSTRAINTS FROM 15N-EDITED NOESY, 13C-EDITED NOESY AND F1-FILTERED/F3-EDITED NOESY SPECTRA, RECORDED ON 13C, 15N-LABELLED SAMPLES IN WHICH ...Text: THE STRUCTURE OF THE COMPLEX WAS DETERMINED USING CONSTRAINTS FROM 15N-EDITED NOESY, 13C-EDITED NOESY AND F1-FILTERED/F3-EDITED NOESY SPECTRA, RECORDED ON 13C, 15N-LABELLED SAMPLES IN WHICH ONLY ONE OF THE TWO COMPONENTS WAS LABELLED

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Sample preparation

DetailsContents: 0.7 MM COMPLEX
Sample conditionsIonic strength: 20 mM / pH: 6.6 / Pressure: 1 atm / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian UNITYPLUSVarianUNITYPLUS5001
Varian UNITYVarianUNITY6002
Varian INOVAVarianINOVA8003
Bruker DRXBrukerDRX8004

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
DYANAstructure solution
X-PLORstructure solution
RefinementMethod: TORSION ANGLE DYNAMICS, CARTESIAN DYANMICS / Software ordinal: 1
Details: REFINEMENT DETAILS MAY BE FOUND IN THE JRNL CITATION ABOVE THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF ALPHA-ACTININ EF34 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. ...Details: REFINEMENT DETAILS MAY BE FOUND IN THE JRNL CITATION ABOVE THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF ALPHA-ACTININ EF34 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE CONSTRAINTS FOR THESE TWO RESIDUES WHICH ARE OMITTED FROM THE STRUCTURE CALCULATION. THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF TITIN ZR7 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE CONSTRAINTS FOR THE N-TERMINAL 8 RESIDUES AND THE C-TERMINAL 22 RESIDUES WHICH ARE OMITTED FROM THE STRUCTURE CALCULATION.
NMR ensembleConformer selection criteria: LOWEST ENERGIES / Conformers calculated total number: 50 / Conformers submitted total number: 30

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