Chemical shift assignments of the canecystatin-1 from Saccharum officinarum.
Cystatins are cysteine proteases inhibitors that are widely distributed among insects, mammalians and plants. Here we report the complete resonance assignment of canecystatin-1 from Saccharum officinarum obtained by heteronuclear multidimensional high-resolution nuclear magnetic resonance spectroscopy. The consensus chemical shift index was calculated and showed the presence of one α-helix (residues 27-43) and three β-strands (residues 48-74, 78-89 and 94-104), a secondary structure pattern that suggests a domain-swapped structure as presented by stefin B and human cystatin C, opposed to the monomeric structure yet found in other phytocystatins like oryza and pineapple cystatin.
Physics Institute of São Carlos, University of São Paulo, Av. Trabalhador Sãocarlense 400, 13566-590 São Carlos, SP, Brazil.
Ítalo Augusto
ÍA
Cavini
Rodrigo
R
de Oliveira-Silva
Ivo
I
de Almeida Marques
Hans Robert
HR
Kalbitzer
Claudia Elisabeth
CE
Munte
D015891:Cystatins / Q000737:chemistry*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D010940:Plant Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D031786:Saccharum / Q000378:metabolism*
D015891:Cystatins; D010940:Plant Proteins; C466627:canecystatin protein, sugarcane