Preliminary crystallographic studies of EcTI, a serine proteinase inhibitor from Enterolobium contortisiliquum seeds.
Enterolobium contortisiliquum trypsin inhibitor (EcTI) belongs to the Kunitz family of plant inhibitors, which are widely distributed in nature, especially in plant seeds. EcTI is composed of two polypeptide chains with a total of 174 residues, homologous to other inhibitors from the same family. EcTI crystals, which were obtained with the acupuncture-gel technique, diffract to 2.0 A resolution and belong to space group P2(1), with unit-cell parameters a = 37.12, b = 38.42, c = 54.08 A, beta = 98.08 degrees. Molecular-replacement techniques using Erythrina caffra trypsin inhibitor (PDB code 1tie) as the search model indicate one monomer in the asymmetric unit. The secondary-structure content of EcTI was determined by circular dichroism spectroscopy, yielding values compatible with the expected topology.
Batista
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Departamento de Bioquímica, Universidade Federal de São Paulo (UNIFESP/EPM), Rua Três de Maio 100, CEP 04044-020 Sao Paulo SP, Brazil. bel.bioq@epm.br
Nonato
M C
MC
Bonfadini
M R
MR
Beltramini
L M
LM
Oliva
M L
ML
Sampaio
M U
MU
Sampaio
C A
CA
Garratt
R C
RC
D002942:Circular Dichroism; D003460:Crystallization; D019684:Magnoliopsida / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012639:Seeds / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry*; D014961:X-Ray Diffraction
D015842:Serine Proteinase Inhibitors