Solution structure of a lipid transfer protein extracted from rice seeds.
Comparison with homologous proteins

Lipid Transfer Protein From Rice Seeds, Nmr, 14 Structures

Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins.

The primary structure of a 9-kDa basic protein from rice seeds was determined by
gas-phase sequencing of the intact protein and peptides derived from it by
digestion with trypsin, chymotrypsin, and endopeptidase Lys-K. The protein
consists of a single polypeptide chain of 91 amino acid residues with a
calculated molecular mass of 8909 Da. It is rich in alanine, serine, glycine,
and cysteine. The eight cysteines form four disulfide bonds. There is no
methionine, histidine, phenylalanine, or tryptophan. The sequence is highly
homologous with an alpha-amylase inhibitor, I-2, from seeds of Indian finger
millet [F. A. P. Campos and M. Richardson (1984) FEBS Lett. 167, 221-225] and a
10-kDa barley seed protein, also called a probable amylase/protease inhibitor
[B. Svensson et al. (1986) Carlsberg Res. Commun. 51, 493-500; J. Mundy and J.
C. Rogers (1986) Planta 169, 51-63]. In analogy with the barley protein, the
purified protein is tentatively called a rice probable amylase/protease
inhibitor (PAPI). The rice PAPI does not show inhibitory activities against
proteases and amylases tested. The amino acid sequence is as follows:
Ile-Thr-Cys-Gly-Gln-Val-Asn-Ser-Ala-Val(10)-Gly-Pro-Cys-Leu-Thr-Tyr-
Ala-Arg-Gly-Gly(20)-Ala-Gly-Pro-Ser-Ala-Ala-Cys-Cys-Ser-Gly(30)-Val-Arg-
Ser-Leu-Lys-Ala-Ala-Ala-Ser-Thr(40)-Thr-Ala-Asp-Arg-Arg-Thr-Ala-Cys-
Asn-Cys(50)-Leu-Lys-Asn-Ala-Ala-Arg-Gly-Ile-Lys-Gly(60)-Leu-Asn-Ala-Gly-
Asn-Ala-Ala-Ser-Ile-Pro(70)-Ser-Lys-Cys-Gly-Val-Ser-Val-Pro-Tyr-Thr(80)-
Ile-Ser-Ala-Ser-Ile-Asp-Cys-Ser-Arg-Val-Ser(91).

Yu YG, Chung CH, Fowler A, Suh SW.
Amino acid sequence of a probable amylase/protease inhibitor from rice seeds.
Arch Biochem Biophys. 1988 Sep;265(2):466-75.

Amino acid sequence of a probable amylase/protease inhibitor from rice seeds.

The program XEASY for computer-supported NMR spectral analysis of biological
macromolecules.

A novel procedure for efficient computation of three-dimensional protein
structures from nuclear magnetic resonance (n.m.r.) data in solution is
described, which is based on using the program DIANA in combination with the
supporting programs CALIBA, HABAS and GLOMSA. The first part of this paper
describes the new programs DIANA. CALIBA and GLOMSA. DIANA is a new, fully
vectorized implementation of the variable target function algorithm for the
computation of protein structures from n.m.r. data. Its main advantages, when
compared to previously available programs using the variable target function
algorithm, are a significant reduction of the computation time, and a novel
treatment of experimental distance constraints involving diastereotopic groups
of hydrogen atoms that were not individually assigned. CALIBA converts the
measured nuclear Overhauser effects into upper distance limits and thus
prepares the input for the previously described program HABAS and for DIANA.
GLOMSA is used for obtaining individual assignments for pairs of diastereotopic
substituents by comparison of the experimental constraints with preliminary
results of the structure calculations. With its general outlay, the presently
used combination of the four programs is particularly user-friendly. In the
second part of the paper, initial results are presented on the influence of the
novel DIANA treatment of diastereotopic protons on the quality of the
structures obtained, and a systematic study of the central processing unit
times needed for the same protein structure calculation on a range of
different, commonly available computers is described.

Guntert P, Braun W, Wuthrich K.
Efficient computation of three-dimensional protein structures in solution from
nuclear magnetic resonance data using the program DIANA and the supporting
programs CALIBA, HABAS and GLOMSA.
J Mol Biol. 1991 Feb 5;217(3):517-30.

Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA.

X-PLOR, version 3.1: A system for X-ray crystallography and NMR

Two NOESY spectra were accumulated with 60 and 200 ms mixing time

simulated annealing in the redac strategy