Complete 1H, 13C, and 15N assignments and secondary structure of the GTPase activating domain of Gs.
Complete 1H, 13C, and 15N assignments for backbone and side-chain atoms of the 145 residue GTPase activating domain of Gs are presented. The combination of gradient-enhanced versions of the HNCACB and CBCA(CO)NNH pulse sequences provided enough information to obtain sequential backbone assignments for residues 2-145 of the polypeptide, as well as assignments of asparagine and glutamine side-chain amides. HBHA(CO)NNH, HCCH-TOCSY, and 13C/15N NOESY-HSQC experiments yielded side-chain 1H and 13C assignments. Chemical shift data and 15N NOESY-HSQC experiments provided information on the secondary structure of the domain, which is similar to that observed in the cognate domain in transducin, a related G protein. The functionally essential C-terminal 15 residues are disordered in solution. These assignments provide a basis for determining the solution structure of the domain.
Benjamin
D R
DR
Department of Pharmaceutical Chemistry, University of California at San Francisco 94143.
Markby
D W
DW
Bourne
H R
HR
Kuntz
I D
ID
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D019204:GTP-Binding Proteins / Q000737:chemistry*; D020690:GTPase-Activating Proteins; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
D002247:Carbon Isotopes; D020690:GTPase-Activating Proteins; D009587:Nitrogen Isotopes; D011506:Proteins; D006859:Hydrogen; D019204:GTP-Binding Proteins