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Titolo:
RICE NONSPECIFIC LIPID TRANSFER PROTEIN - THE 1.6-ANGSTROM CRYSTAL-STRUCTURE IN THE UNLIGANDED STATE REVEALS A SMALL HYDROPHOBIC CAVITY
Autore:
LEE JY; MIN K; CHA H; SHIN DH; HWANG KY; SUH SW;
Indirizzi:
SEOUL NATL UNIV,COLL NAT SCI,DEPT CHEM SEOUL 151742 SOUTH KOREA SEOUL NATL UNIV,COLL NAT SCI,DEPT CHEM SEOUL 151742 SOUTH KOREA
Titolo Testata:
Journal of Molecular Biology
fascicolo: 2, volume: 276, anno: 1998,
pagine: 437 - 448
SICI:
0022-2836(1998)276:2<437:RNLTP->2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; PHOSPHOLIPID TRANSFER PROTEIN; ALPHA-AMYLASE INHIBITOR; INDIAN FINGER MILLET; MACROMOLECULAR STRUCTURES; INTRACELLULAR EXCHANGE; MOLECULAR-REPLACEMENT; MAIZE SEEDLINGS; BARLEY; SEEDS;
Keywords:
NONSPECIFIC LIPID TRANSFER PROTEIN; PROBABLE AMYLASE/PROTEASE INHIBITOR; CRYSTAL STRUCTURE; HYDROPHOBIC CAVITY; RICE PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
J.Y. Lee et al., "RICE NONSPECIFIC LIPID TRANSFER PROTEIN - THE 1.6-ANGSTROM CRYSTAL-STRUCTURE IN THE UNLIGANDED STATE REVEALS A SMALL HYDROPHOBIC CAVITY", Journal of Molecular Biology, 276(2), 1998, pp. 437-448

Abstract

This study describes the high-resolution X-ray structure of the nonspecific lipid transfer protein (ns-LTP) from rice seeds in the unliganded state. The model has been refined to a crystallographic X-factor of0.186 for 8.0 to 1.6 Angstrom data (with F-o > 2 sigma(F)). It accounts for all 91 amino acid residues, 68 water molecules, one sulfate ion, and two molecules of 3-[cyclohexylamino]-1-propanesulfonic acid. Theroot-mean-square deviations from ideal bond lengths and angles are 0.017 Angstrom and 1.76 degrees, respectively. The overall fold of rice ns-LTP is very similar to that of maize ns-LTP. A superposition of 91 common C-alpha atoms in rice and maize ns-LTPs, both in the unligandedstate, gives a root-mean-square deviation of 1.2 Angstrom. Large structural differences from the crystal structure of maize ns-LTPs, are observed in two regions: the loop between two alpha-helices H1 and H2, where one residue deletion (Gln21 of maize sequence) occurs, and the C-terminal region around Tyr79. The C-terminal region of rice protein issomewhat collapsed into the hydrophobic cavity. As a consequence, itshydrophobic cavity is considerably smaller than that of maize protein(144 Angstrom(3) versus 408 Angstrom(3) for van der Waals cavity volumes), despite a high level of sequence identity (79%) between them. Inthe rice ns-LTP structure, the side-chain of Arg44 partially blocks the mouth of the cavity, while the side-chain of Ile81 effectively closes the other end by protruding into the cavity. And the side-chain of Tyr79 divides the cavity into two parts, with the larger part being shielded from the solvent. The present study illuminates the structure-function relationship of rice ns-LTP and allows a detailed structural comparison with other plant ns-LTPs. (C) 1998 Academic Press Limited.

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Documento generato il 11/07/20 alle ore 04:17:44