1H1V Actin-Binding date Jul 23, 2002
title Gelsolin G4-G6actin Complex
authors H.Choe, L.D.Burtnick, M.Mejillano, H.L.Yin, R.C.Robinson, S.Choe
compound source
Molecule: Gelsolin
Synonym: Actin-Depolymerizing Factor, Brevin, Agel
Chain: G
Fragment: G4-G6, Residues 412-742 Of Cytoplasmic Isoform;
Engineered: Yes
 Organism_scientific: Homo Sapiens
Organism_common: Human
Expression_system: Escherichia Coli
Expression_system_strain: Bl21

Molecule: Actin
Chain: A
Organism_scientific: Oryctolagus Cuniculus
Organism_common: Rabbit
Tissue: Muscle
symmetry Space Group: P 21 21 21
R_factor 0.219
crystal
cell
length a length b length c angle alpha angle beta angle gamma
54.350 113.450 159.350 90.00 90.00 90.00
method X-Ray Diffractionresolution 3.0 Å
ligand CA, ATPenzyme
note 1H1V is a representative structure and supersedes 1DB0
related structures by homologous chain: 1D0N, 1IJJ, 1NPH
similarity Contains 6 Gelsolin-like repeats. Belongs to the villin/gelsolin family. Belongs to the actin family.
subunit Polymerization of globular actin (g-actin) leads to a structural filament (f-actin) in the form of a two-stranded helix. Binds to actin and to fibronectin. Each actin can bind to 4 others.
post-translat. modifications Phosphorylation on tyr-86, tyr-409, tyr-465, tyr-603 and tyr- 651 in vitro is induced in presence of phospholipids.
tissue Phagocytic cells, platelets, fibroblasts, nonmuscle cells, smooth and skeletal muscle cells.
subcellular loc. Cytoplasmic. Cytoplasmic (isoform 2); secreted (isoform 1).
genes ACTA, ACTA1, GSN (H. sapiens)
function Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed.
Gene
Ontology 		chain A: GO:0003774, GO:0005198, GO:0005200, GO:0005884, GO:0006936, GO:0007517, GO:0015629
chain G: GO:0003779, GO:0005509, GO:0005576, GO:0005829, GO:0005856, GO:0015629, GO:0030041, GO:0051014, GO:0051016
disease Myopathy,actin
Myopathy,nemaline,161800
Amyloidosis,Finnish type
Defects in gsn are the cause of familial amyloidosis finnish type (faf) [mim. 105120]. Nem is a non-progressive myopathy characterized histologically by abnormal threadlike structures in muscle cells, and clinically by hypotonia with diffuse weakness of the limb and trunk, usually beginning in infancy. Faf is an inherited form of systemic amyloidosis clinically characterized by cranial neuropathy and lattice corneal dystrophy. Defects in acta1 are a cause of congenital myopathy with excess of thin myofilaments (cm) [mim. 102610]. Inheritance can be autosomal dominant (nem1) or recessive (nem2). Defects in acta1 are a cause of nemaline myopathy (nem) [mim. 161800, 256030].
Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (140 Kb) [Save to disk]
  • Biological Unit Coordinates (1h1v.pdb1.gz) 118 Kb
  • LPC: Ligand-Protein Contacts for 1H1V
  • CSU: Contacts of Structural Units for 1H1V
  • Likely Quarternary Molecular Structure file(s) for 1H1V
  • Structure Factors (r1h1vsf.ent.Z) 160 Kb
  • Retrieve 1H1V in mmCIF format [Save to disk]
    • View 1H1V in 3D
  • On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure.
  • On AstexViewer, from MSD-EBI (viewer documentation).
  • On RasMol (Install RasMol freeware) Here's help on how to use RasMol.
    • Visual 3D analysis of 1H1V
  • STING, shows the sequence and maps the locations of sequence residues or residue ranges onto the 3D structure.
  • Noncovalent Bond Finder displays the closest contacts to ligand or interface, reports distances, walks over water bridges.
  • GRASS (Graphical Representation and Analysis of Structure Server)
  • Cartoon representation from PDB Cartoon
  • Ramachandran plot from PDBSum
    • Structure-derived information
  • Electro Density related parameters from EDS Electron Density Server, at Upsala
  • Dipole moment, from Dipole Server at Weizmann Institute
  • Crystal Contacts, from CryCo at Weizmann Institute
  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1h1va2, region A:147-375 [Jmol] [rasmolscript] [script source]
        - Domain d1h1va1, region A:5-146 [Jmol] [rasmolscript] [script source]
        - Domain d1h1vg1, region G:412-532 [Jmol] [rasmolscript] [script source]
        - Domain d1h1vg2, region G:533-628 [Jmol] [rasmolscript] [script source]
        - Domain d1h1vg3, region G:629-742 [Jmol] [rasmolscript] [script source]
  • Fold representative 1h1v from FSSP and Dali (Families of Structurally Similar Proteins)
    • Sequence-derived information
  • View one-letter amino acid or nucleotide sequence for each chain: [1h1v_G] [1h1v_A]
  • SWISS-PROT database: [P02568] [P99020] [Q8WVV7] [P06396]
  • Domain organization of [GELS_HUMAN] [ACTS_HUMAN] by SWISSPFAM
  • Conserved protein region description, domain view and alignment from family Gelsolin (PF00626) of Pfam.
  • Alignments of the sequence of 1H1V with the sequences similar proteins can be viewed for classification [GELS_HUMAN] [ACTS_HUMAN] at ProtoMap. Click on "Neighbors List", then on the "See Alignments" button below the list.
  • A sequence distance tree ("phylogenetic tree") can be viewed for 1ACL's classification [GELS_HUMAN] [ACTS_HUMAN] at ProtoMap. Click on the Cluster number.
    • Other resources with information on 1H1V
  • InterPro: IPR004001 , IPR007122 , IPR007123 , IPR004000
  • MMDB (Entrez's Structure Database)
    • Movements, Movies and Images
  • Images from IMB Jena Image Library of Biological Macromolecules.

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