HOMO-HETERODIMERIC COMPLEX OF THE SRP GTPASES

PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER

Heterodimeric Gtpase Core of the Srp Targeting Complex

Crystallization of the Gmppcp Complex of the Ng Domains of T. Aquaticus Ffh and Ftsy

Conformational Change of the N-Domain on Formation of the Complex between the Gtpase Domains of Thermus Aquaticus Ffh and Ftsy

The Conformation of Bound Gmppnp Suggests a Mechanism for Gating the Active Site of the Srp Gtpase

1.91 M AMMONIUM SULFATE, 0.1 M BISTRIS PH 6.7, 0.1 M NACL, 4% PEG 400.

N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS

T. AQUATICUS FFH NG DOMAIN AT 1.1A RESOLUTION

A NEW MGGDP COMPLEX OF THE FFH NG DOMAIN

STRUCTURE OF THE HETERODIMER OF THE CONSERVED GTPASEDOMAINS OF THE SIGNAL RECOGNITION PARTICLE (FFH) AND ITS RECEPTOR (FTSY)

THE SIGNAL SEQUENCE BINDING PROTEIN FFH FROM THERMUS AQUATICUS

THE UNIPROT ENTRY O07347 HAS ANNOTATION FOR THE INITIAL METHIONINE WHICH IN NOT INCLUDED IN THE SEQUENCE

THE N-TERMINAL THREE RESIDUES OF FFH (A1 - A3) ARE NOT VISIBLE IN THE ELECTRON DENSITY MAP. THE C- TERMINAL RESIDUE OF FFH (A 294) IS DISORDERED AND HAS BEEN OMITTED FROM THE MODEL. THE FIRST 20 AMINO ACIDS OF FTSY (CHAIN D) ARE PROTEOLYTICALLY CLEAVED AND ARE NOT ASSOCIATED WITH THE COMPLEX OR SEEN IN THE CRYSTAL STRUCTURE. FTSY (CHAIN D) IS PROTEOLYTICALLY CLEAVED AT RESIDUE 90, IN THE LINKER BETWEEN THE N AND G DOMAINS. RESIDUES D 79 - D 96 OF THE LINKER REGION ARE NOT VISIBLE IN THE ELECTRON DENSITY MAP. THE C-TERMINAL RESIDUE OF FTSY (D 304) IS NOT VISIBLE IN THE ELECTRON DENSITY MAP. ELECTRON DENSITY FOR FTSY LOOP D60 - D62 IS VERY POORLY DEFINED, AND THE CONFORMATION MAY BE INCORRECT. AN UNUSUAL PARTIAL RING OF ELECTRON DENSITY ENCIRCLES LYS D215 AND HAS BEEN MODELED AS TWO ETHYLENE GLYCOL MOLECULES, BUT SOME POSITIVE DIFFERENCE DENSITY REMAINS

SIGNAL RECOGNITION PARTICLE PROTEIN, CELL DIVISION PROTEIN FTSY

FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK 350

CELL CYCLE, SIGNAL RECOGNITION-COMPLEX, SRP, FFH, FTSY, GTPASE, MEMBRANE TARGETING, SIGNAL SEQUENCE RECOGNITION