Chemical shift assignments of zinc finger domain of methionine aminopeptidase 1 (MetAP1) from Homo sapiens.
Methionine aminopeptidase Type I (MetAP1) cleaves the initiator methionine from about 70 % of all newly synthesized proteins in almost every living cell. Human MetAP1 is a two domain protein with a zinc finger on the N-terminus and a catalytic domain on the C-terminus. Here, we report the chemical shift assignments of the amino terminal zinc binding domain (ZBD) (1-83 residues) of the human MetAP1 derived by using advanced NMR spectroscopic methods. We were able to assign the chemical shifts of ZBD of MetAP1 nearly complete, which reveal two helical fragments involving residues P44-L49 (α1) and Q59-K82 (α2). The protein structure unfolds upon complex formation with the addition of 2 M excess EDTA, indicated by the appearance of amide resonances in the random coil chemical shift region of (15)NHSQC spectrum.
Centre for NMR and Structural Chemistry, CSIR-Indian Institute of Chemical Technology, Uppal Road, Tarnaka, Hyderabad, 500007, India.
Kavitha
K
Rachineni
Centre for Chemical Biology, CSIR-Indian Institute of Chemical Technology, Uppal Road, Tarnaka, Hyderabad, 500007, India.
Tarun
T
Arya
Centre for NMR and Structural Chemistry, CSIR-Indian Institute of Chemical Technology, Uppal Road, Tarnaka, Hyderabad, 500007, India.
Kiran Kumar
KK
Singarapu
Centre for Chemical Biology, CSIR-Indian Institute of Chemical Technology, Uppal Road, Tarnaka, Hyderabad, 500007, India. anthony@iict.res.in.
Anthony
A
Addlagatta
Centre for NMR and Structural Chemistry, CSIR-Indian Institute of Chemical Technology, Uppal Road, Tarnaka, Hyderabad, 500007, India. bj@iict.res.in.
Jagadeesh
J
Bharatam
D000626:Aminopeptidases / Q000737:chemistry*; D006801:Humans; D017434:Protein Structure, Tertiary; D066244:Proton Magnetic Resonance Spectroscopy; D016335:Zinc Fingers
D000626:Aminopeptidases; C506619:METAP1 protein, human
Disordered protein; EDTA; MetAP1; Solution NMR; Zinc binding