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Titolo:
HIGH-RESOLUTION CRYSTAL-STRUCTURE OF THE NONSPECIFIC LIPID-TRANSFER PROTEIN FROM MAIZE SEEDLINGS
Autore:
SHIN DH; LEE JY; HWANG KY; KIM KK; 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:
Structure
fascicolo: 2, volume: 3, anno: 1995,
pagine: 189 - 199
SICI:
0969-2126(1995)3:2<189:HCOTNL>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOLIPID-TRANSFER PROTEIN; AMINO-ACID-SEQUENCE; ALPHA-AMYLASE INHIBITOR; INDIAN FINGER MILLET; ACYL CARRIER PROTEIN; BINDING-PROTEIN; 3-DIMENSIONAL STRUCTURE; BARLEY; PURIFICATION; REFINEMENT;
Keywords:
LIPID TRANSFER PROTEIN; MAIZE PROTEIN; X-RAY STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
49
Recensione:
Indirizzi per estratti:
Citazione:
D.H. Shin et al., "HIGH-RESOLUTION CRYSTAL-STRUCTURE OF THE NONSPECIFIC LIPID-TRANSFER PROTEIN FROM MAIZE SEEDLINGS", Structure, 3(2), 1995, pp. 189-199

Abstract

Background: The movement of lipids between membranes is aided by lipid-transfer proteins (LTPs). Some LTPs exhibit broad specificity, transferring many classes of lipids, and are termed non-specific LTPs (ns-LTPs). Despite their apparently similar mode of action, no sequence homology exists between mammalian and plant ns-LTPs and no three-dimensional structure has been reported for any plant ns-LTP. Results: We havedetermined the crystal structure of ns-LTP from maize seedlings by multiple isomorphous replacement and refined the structure to 1.9 Angstrom resolution. The protein comprises a single compact domain with fouralpha-helices and a long C-terminal region. The eight conserved cysteines form four disulfide bridges (assigned as Cys4-Cys52, Cys14-Cys29,Cys30-Cys75, and Cys50-Cys89) resolving the ambiguity that remained from the chemical determination of pairings in the homologous protein from castor bean. Two of the bonds, Cys4-Cys52 and Cys50-Cys89, differ from what would have been predicted from sequence alignment with soybean hydrophobic protein. The complex between maize ns-LTP and hexadecanoate (palmitate) has also been crystallized and its structure refined to 1.8 Angstrom resolution. Conclusions: The fold of maize ns-LTP places it in a new category of all-alpha-type structure, first described for soybean hydrophobic protein. In the absence of a bound ligand, the protein has a tunnel-like hydrophobic cavity, which is large enough toaccommodate a long fatty acyl chain. In the structure of the complex with palmitate, most of the acyl chain is buried inside this hydrophobic cavity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 16:12:30