PDBsum entry 3tu5

Structural protein/actin-binding protein

PDB id: 3tu5

Contents

Protein chains

370 a.a.

132 a.a.

Ligands

ATP

MPD ×2

Metals

_CA ×2

Waters ×65

PDB id:

3tu5

Name:

Structural protein/actin-binding protein

Title:

Actin complex with gelsolin segment 1 fused to cobl segment

Structure:

Actin, alpha skeletal muscle. Chain: a. Synonym: alpha-actin-1. Gelsolin,protein cordon-bleu,thymosin beta-4. Chain: b. Synonym: agel,actin-depolymerizing factor,adf,brevin,t beta-4,fx. Engineered: yes

Source:

Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Other_details: skeletal. Homo sapiens, mus musculus. Human, mouse. Organism_taxid: 9606, 10090. Gene: gsn, cobl, kiaa0633, tmsb4x, tb4x, thyb4, tmsb4. Expressed in: escherichia coli.

Resolution:

3.00Å R-factor: 0.167 R-free: 0.205

Authors:

D.S.Kudryashov,M.R.Sawaya,Z.A.O.Durer

Key ref:

Z.A.Durer et al. (2012). Structural states and dynamics of the D-loop in actin. Biophys J, 103, 930-939. PubMed id: 23009842

Date:

15-Sep-11 Release date: 26-Sep-12

Protein chain

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

Seq: 377 a.a.

Struc: 370 a.a.

Protein chain

P06396  (GELS_HUMAN) -  Gelsolin from Homo sapiens

Seq: 782 a.a.

Struc: 132 a.a.*

Protein chain

P62328  (TYB4_HUMAN) -  Thymosin beta-4 from Homo sapiens

Seq: 44 a.a.

Struc: 132 a.a.*

Protein chain

Q5NBX1  (COBL_MOUSE) -  Protein cordon-bleu from Mus musculus

Seq: 1337 a.a.

Struc: 132 a.a.*

* PDB and UniProt seqs differ at 151 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chain A: E.C.3.6.4.- - ?????
• Enzyme class 2: 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.

Biophys J 103:930-939 (2012)

PubMed id: 23009842

Structural states and dynamics of the D-loop in actin.

Z.A.Durer, D.S.Kudryashov, M.R.Sawaya, C.Altenbach, W.Hubbell, E.Reisler.

ABSTRACT

Conformational changes induced by ATP hydrolysis on actin are involved in the regulation of complex actin networks. Previous structural and biochemical data implicate the DNase I binding loop (D-loop) of actin in such nucleotide-dependent changes. Here, we investigated the structural and conformational states of the D-loop (in solution) using cysteine scanning mutagenesis and site-directed labeling. The reactivity of D-loop cysteine mutants toward acrylodan and the mobility of spin labels on these mutants do not show patterns of an α-helical structure in monomeric and filamentous actin, irrespective of the bound nucleotide. Upon transition from monomeric to filamentous actin, acrylodan emission spectra and electron paramagnetic resonance line shapes of labeled mutants are blue-shifted and more immobilized, respectively, with the central residues (residues 43-47) showing the most drastic changes. Moreover, complex electron paramagnetic resonance line shapes of spin-labeled mutants suggest several conformational states of the D-loop. Together with a new (to our knowledge) actin crystal structure that reveals the D-loop in a unique hairpin conformation, our data suggest that the D-loop equilibrates in F-actin among different conformational states irrespective of the nucleotide state of actin.