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PDBsum entry 1eqk
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Hydrolase inhibitor
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PDB id
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1eqk
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Three-Dimensional solution structure of oryzacystatin-I, A cysteine proteinase inhibitor of the rice, Oryza sativa l. Japonica.
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Authors
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K.Nagata,
N.Kudo,
K.Abe,
S.Arai,
M.Tanokura.
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Ref.
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Biochemistry, 2000,
39,
14753-14760.
[DOI no: ]
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PubMed id
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Abstract
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The three-dimensional structure of oryzacystatin-I, a cysteine proteinase
inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution
at pH 6.8 and 25 degrees C by (1)H and (15)N NMR spectroscopy. The main body
(Glu13-Asp97) of oryzacystatin-I is well-defined and consists of an alpha-helix
and a five-stranded antiparallel beta-sheet, while the N- and C-terminal regions
(Ser2-Val12 and Ala98-Ala102) are less defined. The helix-sheet architechture of
oryzacystatin-I is stabilized by a hydrophobic cluster formed between the
alpha-helix and the beta-sheet and is considerably similar to that of monellin,
a sweet-tasting protein from an African berry, as well as those of the animal
cystatins studied, e.g., chicken egg white cystatin and human stefins A and B
(also referred to as human cystatins A and B). Detailed structural comparison
indicates that oryzacystatin-I is more similar to chicken cystatin, which
belongs to the type-2 animal cystatins, than to human stefins A and B, which
belong to the type-1 animal cystatins, despite different loop length.
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