PDBsum entry 1cz7

Contractile protein

PDB id: 1cz7

Contents

Protein chains

342 a.a. *

364 a.a. *

Ligands

ADP ×4

Metals

_MG ×4

Waters ×148

* Residue conservation analysis

PDB id:

1cz7

Name:

Contractile protein

Title:

The crystal structure of a minus-end directed microtubule motor protein ncd reveals variable dimer conformations

Structure:

Microtubule motor protein ncd. Chain: a, b, c, d. Fragment: construct mc5 from ncd. Synonym: ncd, claret segregational protein. Engineered: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.90Å R-factor: 0.258 R-free: 0.294

Authors:

F.K.Kozielski,S.De Bonis,W.Burmeister,C.Cohen-Addad,R.Wade

Key ref:

F.Kozielski et al. (1999). The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations. Structure, 7, 1407-1416. PubMed id: 10574799 DOI: 10.1016/S0969-2126(00)80030-1

Date:

01-Sep-99 Release date: 05-Nov-99

Protein chains

P20480  (NCD_DROME) -  Protein claret segregational from Drosophila melanogaster

Seq: 700 a.a.

Struc: 342 a.a.

Protein chains

P20480  (NCD_DROME) -  Protein claret segregational from Drosophila melanogaster

Seq: 700 a.a.

Struc: 364 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.3.6.4.- - ?????

DOI no: 10.1016/S0969-2126(00)80030-1

Structure 7:1407-1416 (1999)

PubMed id: 10574799

The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations.

F.Kozielski, S.De Bonis, W.P.Burmeister, C.Cohen-Addad, R.H.Wade.

ABSTRACT

BACKGROUND: The kinesin superfamily of microtubule-associated motor proteins are important for intracellular transport and for cell division in eukaryotes. Conventional kinesins have the motor domain at the N terminus of the heavy chain and move towards the plus end of microtubules. The ncd protein is necessary for chromosome segregation in meiosis. It belongs to a subfamily of kinesins that have the motor domain at the C terminus and move towards the minus end of microtubules. RESULTS: The crystal structure of dimeric ncd has been obtained at 2.9 A resolution from crystals with the C222(1) space group, with two independent dimers per asymmetric unit. The motor domains in these dimers are not related by crystallographic symmetry and the two ncd dimers have significantly different conformations. An alpha-helical coiled coil connects, and interacts with, the motor domains. CONCLUSIONS: The ncd protein has a very compact structure, largely due to extended interactions of the coiled coil with the head domains. Despite this, we find that the overall conformation of the ncd dimer can be rotated by as much as 10 degrees away from that of the twofold-symmetric archetypal ncd. The crystal structures of conventional kinesin and of ncd suggest a structural rationale for the reversal of the direction of movement in chimeric kinesins.

Selected figure(s)

Figure 1.
Figure 1. The overall fold of the ncd dimer. (a) Schematic representation of the ncd conformation and of the polypeptide chain with the secondary structure elements visible in the crystal structure, following the nomenclature in [9]. The sequence in the coiled-coil helix is shown below. (b) Stereoview of the C[a] backbone of the Drosophila melanogaster ncd dimer 1. Every twentieth residue and also the N termini (N) and the C termini of the two head domains are labelled. (c) Stereoview of the structure of dimer 1. Helices of the first head domain are coloured in orange and b strands are in light blue. In the second head domain, helices are in red and b strands are dark blue. The MgADP in the active site is shown as a ball-and-stick model. This and the following figures were prepared with the program MOLSCRIPT [32].

The above figure is reprinted by permission from Cell Press: Structure (1999, 7, 1407-1416) copyright 1999.

Figure was selected by an automated process.