Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins.
The surface layer of archaeobacteria protects cells from extreme environments and, in Methanosarcina, may regulate cell adhesion. We identify three domain types that account for the complete architecture of numerous Methanosarcina surface layer proteins (SLPs). We solve the crystal structure for two of these domains, which correspond to the two N-terminal domains of an M. mazei SLP. One domain displays a unique, highly symmetrical, seven-bladed beta propeller fold, and the other belongs to the polycystic kidney disease (PKD) superfamily fold. The third domain is predicted to adopt a beta helix fold. These domains have homologs in metazoan cell surface proteins, suggesting remarkable relationships between domains in archaeal SLPs and metazoan cell surface proteins.
Jing
Hua
H
Center for Blood Research and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
Takagi
Junichi
J
Liu
Jin-huan
JH
Lindgren
Sara
S
Zhang
Rong-guang
RG
Joachimiak
A
A
Wang
Jia-huai
JH
Springer
Timothy A
TA
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D008565:Membrane Proteins