PMID- 10574799
OWN - NLM
STAT- MEDLINE
DCOM- 19991214
LR  - 20211203
IS  - 0969-2126 (Print)
IS  - 0969-2126 (Linking)
VI  - 7
IP  - 11
DP  - 1999 Nov 15
TI  - The crystal structure of the minus-end-directed microtubule motor protein ncd
      reveals variable dimer conformations.
PG  - 1407-16
AB  - 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.
FAU - Kozielski, F
AU  - Kozielski F
AD  - Institut de Biologie Structurale (CEA/CNRS), Grenoble, 38027, France.
FAU - De Bonis, S
AU  - De Bonis S
FAU - Burmeister, W P
AU  - Burmeister WP
FAU - Cohen-Addad, C
AU  - Cohen-Addad C
FAU - Wade, R H
AU  - Wade RH
LA  - eng
SI  - PDB/1CZ7
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Structure
JT  - Structure (London, England : 1993)
JID - 101087697
RN  - 0 (Drosophila Proteins)
RN  - 0 (ncd protein, Drosophila)
RN  - 61D2G4IYVH (Adenosine Diphosphate)
RN  - EC 3.6.4.4 (Kinesins)
SB  - IM
MH  - Adenosine Diphosphate/metabolism
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Catalysis
MH  - Crystallography, X-Ray
MH  - Dimerization
MH  - *Drosophila Proteins
MH  - Kinesins/*chemistry/metabolism
MH  - Molecular Sequence Data
MH  - Protein Conformation
EDAT- 1999/11/27 00:00
MHDA- 1999/11/27 00:01
CRDT- 1999/11/27 00:00
PHST- 1999/11/27 00:00 [pubmed]
PHST- 1999/11/27 00:01 [medline]
PHST- 1999/11/27 00:00 [entrez]
AID - S0969-2126(00)80030-1 [pii]
AID - 10.1016/s0969-2126(00)80030-1 [doi]
PST - ppublish
SO  - Structure. 1999 Nov 15;7(11):1407-16. doi: 10.1016/s0969-2126(00)80030-1.