A molecular modeling study of the interaction between SRP-receptor complex and peptide translocon.
The signal recognition particle (SRP) mediated protein translocation pathway is universal and highly conserved in all kingdoms of life. Significant progresses have been made to understand its molecular mechanism, yet many open questions remain. A structure model, showing how nascent peptide inserts into peptide translocon with the help of SRP protein Ffh and its receptor FtsY, is desired to facilitate our studies. In this work, we presented such a model derived by computational docking of the Ffh-FtsY complex onto the translocon. This model was compatible with most available experiments. It suggested that the Ffh-FtsY complex approached the translocon with its G domains and was locked up by the cytoplasmic loop of SecG and the C5/C6 loops of SecY. Several residues were expected to play important roles in regulating GTP hydrolysis. Additionally, a hypothesis on the yet ambiguous function of FtsY A domain was proposed. These interesting results invite experimental investigations.
Institute of Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, PR China.
Shifei
S
Chen
Institute of Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, PR China.
Yi
Y
Fan
Institute of Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, PR China.
Xueling
X
Shen
Department of Bioinformatics, Zhejiang University, Zijingang Campus, 358 Zijinhua Road, Hangzhou, Zhejiang 310058, PR China.
Peng
P
Sun
Hangzhou Vocational & Technical College, Hangzhou, Zhejiang 310018, PR China.
Guosong
G
Jiang
Hangzhou Vocational & Technical College, Hangzhou, Zhejiang 310018, PR China.
Yi
Y
Shen
Institute of Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, PR China.
Wenfei
W
Xue
Institute of Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, PR China. Electronic address: lyq@zju.edu.cn.
Yongquan
Y
Li
Department of Bioinformatics, Zhejiang University, Zijingang Campus, 358 Zijinhua Road, Hangzhou, Zhejiang 310058, PR China. Electronic address: xinchen@zju.edu.cn.
Xin
X
Chen
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003198:Computer Simulation; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018000:Receptors, Peptide / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018271:Signal Recognition Particle / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D029968:Escherichia coli Proteins; C082931:Ffh protein, E coli; C087406:FtsY protein, Bacteria; D008562:Membrane Glycoproteins; D018160:Receptors, Cytoplasmic and Nuclear; D018000:Receptors, Peptide; D018271:Signal Recognition Particle; C066973:signal sequence receptor