PDBsum entry 4pd3

Contractile protein

PDB id: 4pd3

Contents

Protein chains

922 a.a.

Waters ×33

PDB id:

4pd3

Name:

Contractile protein

Title:

Crystal structure of rigor-like human nonmuscle myosin-2b

Structure:

Nonmuscle myosin heavy chain b, alpha-actinin a chimera protein. Chain: a, b. Fragment: unp p35580 residues 1-782, unp p05095 residues 265-502. Synonym: cellular myosin heavy chain,type b,myosin heavy chain 10, myosin heavy chain,non-muscle iib,non-muscle myosin heavy chain b, nmmhc-b,non-muscle myosin heavy chain iib,nmmhc-iib,actin-binding protein a,f-actin cross-linking protein. Engineered: yes

Source:

Homo sapiens, dictyostelium discoideum. Human, slime mold. Organism_taxid: 9606, 44689. Gene: myh10, abpa, actna, ddb_g0268632. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.

Resolution:

2.84Å R-factor: 0.254 R-free: 0.288

Authors:

S.Munnich,S.Pathan-Chhatbar,D.J.Manstein

Key ref:

S.Münnich et al. (2014). Crystal structure of the rigor-like human non-muscle myosin-2 motor domain. Febs Lett, 588, 4754-4760. PubMed id: 25451231 DOI: 10.1016/j.febslet.2014.11.007

Date:

17-Apr-14 Release date: 12-Nov-14

Protein chains

P05095  (ACTNA_DICDI) -  Alpha-actinin A from Dictyostelium discoideum

Seq: 861 a.a.

Struc: 922 a.a.*

Protein chains

P35580  (MYH10_HUMAN) -  Myosin-10 from Homo sapiens

Seq: 1976 a.a.

Struc: 922 a.a.*

* PDB and UniProt seqs differ at 437 residue positions (black crosses)

DOI no: 10.1016/j.febslet.2014.11.007

Febs Lett 588:4754-4760 (2014)

PubMed id: 25451231

Crystal structure of the rigor-like human non-muscle myosin-2 motor domain.

S.Münnich, S.Pathan-Chhatbar, D.J.Manstein.

ABSTRACT

We determined the crystal structure of the motor domain of human non-muscle myosin 2B (NM-2B) in a nucleotide-free state and at a resolution of 2.8Å. The structure shows the motor domain with an open active site and the large cleft that divides the 50kDa domain in a closed state. Compared to other rigor-like myosin motor domain structures, our structure shows subtle but significant conformational changes in regions important for actin binding and mechanochemical coupling. Moreover, our crystal structure helps to rationalize the impact of myosin, heavy chain 9 (MYH9)-related disease mutations Arg709Cys and Arg709His on the kinetic and functional properties of NM-2B and of the closely related non-muscle myosin 2A (NM-2A).