PDBsum entry 4atx

Hydrolase

PDB id: 4atx

Contents

Protein chains

426 a.a.

429 a.a.

310 a.a.

Ligands

GDP

GTP

PDB id:

4atx

Name:

Hydrolase

Title:

Rigor kinesin motor domain with an ordered neck-linker, docked on tubulin dimer, modelled into the 8a cryo-em map of doublecortin- microtubules decorated with kinesin

Structure:

Tubulin beta-2b chain. Chain: a. Tubulin alpha-1d chain. Chain: b. Kinesin-1 heavy chain. Chain: c. Fragment: motor domain, residues 1-340. Synonym: conventional kinesin heavy chain, ubiquitous kinesin heavy chain, ukhc.

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Organ: brain. Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562

Authors:

J.S.Liu,C.R.Schubert,X.Fu,F.J.Fourniol,J.K.Jaiswal,A.Houdusse, C.M.Stultz,C.A.Moores,C.A.Walsh

Key ref:

J.S.Liu et al. (2012). Molecular basis for specific regulation of neuronal kinesin-3 motors by doublecortin family proteins. Mol Cell, 47, 707-721. PubMed id: 22857951

Date:

10-May-12 Release date: 26-Sep-12

Protein chain

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

Seq: 445 a.a.

Struc: 426 a.a.*

Protein chain

Q2HJ86  (TBA1D_BOVIN) -  Tubulin alpha-1D chain from Bos taurus

Seq: 452 a.a.

Struc: 429 a.a.*

Protein chain

Q2PQA9  (KINH_RAT) -  Kinesin-1 heavy chain from Rattus norvegicus

Seq: 963 a.a.

Struc: 310 a.a.*

* PDB and UniProt seqs differ at 12 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chain A: E.C.3.6.5.6 - tubulin GTPase.
• Reaction: GTP + H2O = GDP + phosphate + H⁺

GTP (Bound ligand (Het Group name = GTP) corresponds exactly) + H2O = GDP (Bound ligand (Het Group name = GDP) corresponds exactly) + phosphate + H(+)

• Enzyme class 2: Chain B: E.C.3.6.5.- - ?????
• Enzyme class 3: Chain C: E.C.3.6.4.4 - Transferred entry: 5.6.1.3.
• Reaction: ATP + H₂O = ADP + phosphate

ATP + H(2)O = ADP (Bound ligand (Het Group name = GDP) matches with 96.43% similarity) + phosphate

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.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Mol Cell 47:707-721 (2012)

PubMed id: 22857951

Molecular basis for specific regulation of neuronal kinesin-3 motors by doublecortin family proteins.

J.S.Liu, C.R.Schubert, X.Fu, F.J.Fourniol, J.K.Jaiswal, A.Houdusse, C.M.Stultz, C.A.Moores, C.A.Walsh.

ABSTRACT

Doublecortin (Dcx) defines a growing family of microtubule (MT)-associated proteins (MAPs) involved in neuronal migration and process outgrowth. We show that Dcx is essential for the function of Kif1a, a kinesin-3 motor protein that traffics synaptic vesicles. Neurons lacking Dcx and/or its structurally conserved paralogue, doublecortin-like kinase 1 (Dclk1), show impaired Kif1a-mediated transport of Vamp2, a cargo of Kif1a, with decreased run length. Human disease-associated mutations in Dcx's linker sequence (e.g., W146C, K174E) alter Kif1a/Vamp2 transport by disrupting Dcx/Kif1a interactions without affecting Dcx MT binding. Dcx specifically enhances binding of the ADP-bound Kif1a motor domain to MTs. Cryo-electron microscopy and subnanometer-resolution image reconstruction reveal the kinesin-dependent conformational variability of MT-bound Dcx and suggest a model for MAP-motor crosstalk on MTs. Alteration of kinesin run length by MAPs represents a previously undiscovered mode of control of kinesin transport and provides a mechanism for regulation of MT-based transport by local signals.