1FWO

THE SOLUTION STRUCTURE OF A 35-RESIDUE FRAGMENT FROM THE GRANULIN/EPITHELIN-LIKE SUBDOMAIN OF RICE ORYZAIN BETA (ROB 382-416 (C398S,C399S,C407S,C413S))

Summary for 1FWO

• Entry DOI: 10.2210/pdb1fwo/pdb
• Related: 1QGM
• NMR Information: BMRB: 4645
• Descriptor: ORYZAIN BETA CHAIN (1 entity in total)
• Functional Keywords: beta-hairpin stack fold, granulin/epithelin-like protein repeats, hydrolase
• Total number of polymer chains: 1
• Total formula weight: 3711.06

Authors

Tolkatchev, D.,Xu, P.,Ni, F. (deposition date: 2000-09-24, release date: 2001-05-09, Last modification date: 2024-10-30)

Primary citation

Tolkatchev, D.,Xu, P.,Ni, F.
A peptide derived from the C-terminal part of a plant cysteine protease folds into a stack of two beta-hairpins, a scaffold present in the emerging family of granulin-like growth factors.
J.Pept.Res., 57:227-233, 2001

PubMed Abstract: A 35 amino acid residue peptide corresponding to the N-terminal subdomain of the granulin-like repeat from rice oryzain beta was synthesized and regioselectively oxidized to produce a species with a [1-3, 2-4] disulfide-pairing pattern. The resulting peptide was studied in solution using NMR and was shown to adopt the tertiary topology of a stack of two beta-hairpins found in the emerging family of granulin-like growth factors. Because of the longer second beta-hairpin, the overall conformation of the peptide is somewhat more flexible than that of its well-structured carp granulin-1 analog. Except for the cysteine alignment, there is very little sequence homology between granulin-like growth factors from the animal kingdom and the granulin-like repeats at the C-termini of plant cysteine proteases. Therefore, the stack of two beta-hairpins may be a conserved three-dimensional organization of the granulin-like repeats from evolutionary distant sources with a significant role in specific protein-protein interactions.

PubMed: 11298924

Experimental method

SOLUTION NMR