PDBsum entry 4uxs

Transport protein

PDB id: 4uxs

Contents

Protein chains

412 a.a.*

426 a.a.*

340 a.a.*

Ligands

GTP

GDP

TA1

Metals

_ZN

_MG

* C-alpha coords only

PDB id:

4uxs

Name:

Transport protein

Title:

Conserved mechanisms of microtubule-stimulated adp release, atp binding, and force generation in transport kinesins

Structure:

Tubulin alpha-1b chain. Chain: a. Synonym: alpha-tubulin ubiquitous. Tubulin beta-2b chain. Chain: b. Kinesin-3 motor domain. Chain: c. Engineered: yes

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

Authors:

J.Atherton,I.Farabella,I.M.Yu,S.S.Rosenfeld,A.Houdusse,M.Topf, C.Moores

Key ref:

J.Atherton et al. (2014). Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins. Elife, 3, e03680. PubMed id: 25209998 DOI: 10.7554/eLife.03680

Date:

27-Aug-14 Release date: 24-Sep-14

Protein chain

P81947  (TBA1B_BOVIN) -  Tubulin alpha-1B chain from Bos taurus

Seq: 451 a.a.

Struc: 412 a.a.*

Protein chain

Q6B856  (TBB2B_BOVIN) -  Tubulin beta-2B chain from Bos taurus

Seq: 445 a.a.

Struc: 426 a.a.*

Protein chain

Q12756  (KIF1A_HUMAN) -  Kinesin-like protein KIF1A from Homo sapiens

Seq: 1690 a.a.

Struc: 340 a.a.

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chain A: E.C.3.6.5.- - ?????
• Enzyme class 3: Chains B, C: 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.

DOI no: 10.7554/eLife.03680

Elife 3:e03680 (2014)

PubMed id: 25209998

Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins.

J.Atherton, I.Farabella, I.M.Yu, S.S.Rosenfeld, A.Houdusse, M.Topf, C.A.Moores.

ABSTRACT

Kinesins are a superfamily of microtubule-based ATP-powered motors, important for multiple, essential cellular functions. How microtubule binding stimulates their ATPase and controls force generation is not understood. To address this fundamental question, we visualized microtubule-bound kinesin-1 and kinesin-3 motor domains at multiple steps in their ATPase cycles--including their nucleotide-free states--at ∼ 7 Å resolution using cryo-electron microscopy. In both motors, microtubule binding promotes ordered conformations of conserved loops that stimulate ADP release, enhance microtubule affinity and prime the catalytic site for ATP binding. ATP binding causes only small shifts of these nucleotide-coordinating loops but induces large conformational changes elsewhere that allow force generation and neck linker docking towards the microtubule plus end. Family-specific differences across the kinesin-microtubule interface account for the distinctive properties of each motor. Our data thus provide evidence for a conserved ATP-driven mechanism for kinesins and reveal the critical mechanistic contribution of the microtubule interface.