Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain.
Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three beta-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.
Li
Songlin
S
Southeast Collaboratory for Structural Genomics, University of Georgia, Athens 30602, USA.
Finley
Jim
J
Liu
Zhi-Jie
ZJ
Qiu
Shi-Hong
SH
Chen
Hongli
H
Luan
Chi-Hao
CH
Carson
Mike
M
Tsao
Jun
J
Johnson
David
D
Lin
Guangda
G
Zhao
Jun
J
Thomas
Willie
W
Nagy
Lisa A
LA
Sha
Bingdong
B
DeLucas
Lawrence J
LJ
Wang
Bi-Cheng
BC
Luo
Ming
M
D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000737:chemistry; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D003598:Cytoskeletal Proteins / Q000737:chemistry*; D005998:Glycine / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D029742:Caenorhabditis elegans Proteins; D003598:Cytoskeletal Proteins; D005998:Glycine