| Autor: |
Gomar J; Centre de Biophysique Moléculaire, Orléans, France., Sodano P, Sy D, Shin DH, Lee JY, Suh SW, Marion D, Vovelle F, Ptak M |
| Jazyk: |
angličtina |
| Zdroj: |
Proteins [Proteins] 1998 May 01; Vol. 31 (2), pp. 160-71. |
| DOI: |
10.1002/(sici)1097-0134(19980501)31:2<160::aid-prot6>3.0.co;2-q |
| Abstrakt: |
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: |
MEDLINE |
| Externí odkaz: |
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