Comparison of solution and crystal structures of maize nonspecific lipid transfer protein: A model for a potential in vivo lipid carrier protein
| Autor: | Didier Marion, Patrick Sodano, Françoise Vovelle, Jérôme Gomar, Denise Sy, Dong Hae Shin, Marius Ptak, Se Won Suh, Jae Young Lee |
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| Přispěvatelé: | UR 0724 Unité de recherche Biochimie et technologie des protéines, Institut National de la Recherche Agronomique (INRA)-Transformation des Produits Végétaux (T.P.V.)-Unité de recherche Biochimie et technologie des protéines (NANT LBTP), ProdInra, Migration |
| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular Protein Folding Magnetic Resonance Spectroscopy CRYSTALLOGRAPHIE Molecular model Protein Conformation [SDV]Life Sciences [q-bio] Molecular Sequence Data Crystal structure Crystallography X-Ray Zea mays Biochemistry MODELISATION MOLECULAIRE Species Specificity Structural Biology In vivo Molecule Amino Acid Sequence Molecular Biology Plant Proteins Sequence Homology Amino Acid Chemistry Hydrogen bond Intermolecular force [SDV] Life Sciences [q-bio] Crystallography Solubility Docking (molecular) PROTEINE DE TRANSFERT DE LIPIDE Carrier Proteins Crystallization Sequence Alignment Plant lipid transfer proteins |
| Zdroj: | Proteins-Structure, Function and Bioinformatics Proteins-Structure, Function and Bioinformatics, Wiley, 1998, 31, pp.160-171 |
| ISSN: | 1097-0134 0887-3585 |
| DOI: | 10.1002/(sici)1097-0134(19980501)31:2<160::aid-prot6>3.0.co;2-q |
| Popis: | The three-dimensional solution structure of maize nonspecific lipid transfer protein (nsLTP) obtained by nuclear magnetic resonance (NMR) is compared to the X-ray structure. Although both structures are very similar, some local structural differences are observed in the first and the fourth helices and in several side-chain conformations. These discrepancies arise partly from intermolecular contacts in the crystal lattice. The main characteristic of nsLTP structures is the presence of an internal hydrophobic cavity whose volume was found to vary from 237 to 513 A3 without major variations in the 15 solution structures. Comparison of crystal and NMR structures shows the existence of another small hollow at the periphery of the protein containing a water molecule in the X-ray structure, which could play an important structural role. A model of the complexed form of maize nsLTP by alpha-lysopalmitoylphosphatidylcholine was built by docking the lipid inside the protein cavity of the NMR structure. The main structural feature is a hydrogen bond found also in the X-ray structure of the complex maize nsLTP/palmitate between the hydroxyl of Tyr81 and the carbonyl of the lipid. Comparison of 12 primary sequences of nsLTPs emphasizes that all residues delineating the cavities calculated on solution and X-ray structures are conserved, which suggests that this large cavity is a common feature of all compared plant nsLTPs. Furthermore several conserved basic residues seem to be involved in the stabilization of the protein architecture. |
| Databáze: | OpenAIRE |
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