PDBsum entry 3sjh

Contractile protein, protein binding

PDB id: 3sjh

Contents

Protein chains

357 a.a.

22 a.a.

Ligands

ATP

LAR

Metals

_MG

Waters ×359

PDB id:

3sjh

Name:

Contractile protein, protein binding

Title:

Crystal structure of a chimera containing the n-terminal domain (residues 8-29) of drosophila ciboulot and thE C-terminal domain (residues 18-44) of bovine thymosin-beta4, bound to g-actin-atp- latrunculin a

Structure:

Actin, alpha skeletal muscle. Chain: a. Fragment: unp residues 3-377. Synonym: alpha-actin-1. Ciboulot/thymosin beta-4 chimeric protein. Chain: b. Fragment: unp o97428 residues 8-29, unp p62326 residues 18-44. Synonym: ciboulot, isoform b, eg:eg0007.11 protein, re50273p. Engineered: yes

Source:

Oryctolagus cuniculus. European rabbit,japanese white rabbit,domestic rabbit,rabbits. Organism_taxid: 9986. Organ: alpha skeletal muscle. Drosophila melanogaster, bos taurus. Organism_taxid: 7227, 9913. Gene: cib, eg:eg0007.11, cg4944, dmel_cg4944. Expressed in: escherichia coli.

Resolution:

1.75Å R-factor: 0.171 R-free: 0.199

Authors:

L.Renault,C.Husson,M.F.Carlier,D.Didry

Key ref:

D.Didry et al. (2012). How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly. Embo J, 31, 1000-1013. PubMed id: 22193718

Date:

21-Jun-11 Release date: 25-Jan-12

Protein chain

P68135  (ACTS_RABIT) -  Actin, alpha skeletal muscle from Oryctolagus cuniculus

Seq: 377 a.a.

Struc: 357 a.a.

Protein chain

O97428  (O97428_DROME) -  Ciboulot, isoform A from Drosophila melanogaster

Seq: 129 a.a.

Struc: 22 a.a.*

Protein chain

P62326  (TYB4_BOVIN) -  Thymosin beta-4 from Bos taurus

Seq: 44 a.a.

Struc: 22 a.a.*

* PDB and UniProt seqs differ at 16 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chain A: E.C.3.6.4.- - ?????
• Enzyme class 3: Chain B: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Embo J 31:1000-1013 (2012)

PubMed id: 22193718

How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly.

D.Didry, F.X.Cantrelle, C.Husson, P.Roblin, A.M.Moorthy, J.Perez, C.Le Clainche, M.Hertzog, E.Guittet, M.F.Carlier, C.van Heijenoort, L.Renault.

ABSTRACT

No abstract given.