PDBsum entry 4w8f

Motor protein

PDB id: 4w8f

Contents

Protein chains

2608 a.a.

Ligands

ANP ×8

Metals

_MG ×2

PDB id:

4w8f

Name:

Motor protein

Title:

Crystal structure of the dynein motor domain in the amppnp-bound state

Structure:

Dynein heavy chain lysozyme chimera. Chain: a, b. Synonym: dynein heavy chain,cytosolic,dyhc,lysis protein,muramidase. Engineered: yes. Mutation: yes

Source:

Saccharomyces cerevisiae, enterobacteria phage t4. Baker's yeast. Organism_taxid: 559292, 10665. Strain: atcc 204508 / s288c. Gene: dyn1, dhc1, ykr054c. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932

Resolution:

3.54Å R-factor: 0.230 R-free: 0.262

Authors:

H.-C.Cheng,G.Bhabha,N.Zhang,R.D.Vale

Key ref:

G.Bhabha et al. (2014). Allosteric communication in the dynein motor domain. Cell, 159, 857-868. PubMed id: 25417161 DOI: 10.1016/j.cell.2014.10.018

Date:

24-Aug-14 Release date: 12-Nov-14

Protein chains

P00720  (ENLYS_BPT4) -  Endolysin from Enterobacteria phage T4

Seq: 164 a.a.

Struc: 2608 a.a.*

Protein chains

P36022  (DYHC_YEAST) -  Dynein heavy chain, cytoplasmic from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 4092 a.a.

Struc: 2608 a.a.*

* PDB and UniProt seqs differ at 137 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.2.1.17 - lysozyme.
• Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

DOI no: 10.1016/j.cell.2014.10.018

Cell 159:857-868 (2014)

PubMed id: 25417161

Allosteric communication in the dynein motor domain.

G.Bhabha, H.C.Cheng, N.Zhang, A.Moeller, M.Liao, J.A.Speir, Y.Cheng, R.D.Vale.

ABSTRACT

Dyneins power microtubule motility using ring-shaped, AAA-containing motor domains. Here, we report X-ray and electron microscopy (EM) structures of yeast dynein bound to different ATP analogs, which collectively provide insight into the roles of dynein's two major ATPase sites, AAA1 and AAA3, in the conformational change mechanism. ATP binding to AAA1 triggers a cascade of conformational changes that propagate to all six AAA domains and cause a large movement of the "linker," dynein's mechanical element. In contrast to the role of AAA1 in driving motility, nucleotide transitions in AAA3 gate the transmission of conformational changes between AAA1 and the linker, suggesting that AAA3 acts as a regulatory switch. Further structural and mutational studies also uncover a role for the linker in regulating the catalytic cycle of AAA1. Together, these results reveal how dynein's two major ATP-binding sites initiate and modulate conformational changes in the motor domain during motility.