1afh
From Proteopedia
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| - | [[Image:1afh.gif|left|200px]] | + | [[Image:1afh.gif|left|200px]] |
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| - | '''LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1afh |SIZE=350|CAPTION= <scene name='initialview01'>1afh</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AFH is a [ | + | 1AFH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFH OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds., Gomar J, Petit MC, Sodano P, Sy D, Marion D, Kader JC, Vovelle F, Ptak M, Protein Sci. 1996 Apr;5(4):565-77. PMID:[http:// | + | Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds., Gomar J, Petit MC, Sodano P, Sy D, Marion D, Kader JC, Vovelle F, Ptak M, Protein Sci. 1996 Apr;5(4):565-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8845747 8845747] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:56:48 2008'' |
Revision as of 07:56, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES
Overview
The three-dimensional solution structure of a nonspecific lipid transfer protein extracted from maize seeds determined by 1H NMR spectroscopy is described. This cationic protein consists of 93 amino acid residues. Its structure was determined from 1,091 NOE-derived distance restraints, including 929 interresidue connectivities and 197 dihedral restraints (phi, psi, chi 1) derived from NOEs and 3J coupling constants. The global fold involving four helical fragments connected by three loops and a C-terminal tail without regular secondary structures is stabilized by four disulfide bridges. The most striking feature of this structure is the existence of an internal hydrophobic cavity running through the whole molecule. The global fold of this protein, very similar to that of a previously described lipid transfer protein extracted from wheat seeds (Gincel E et al., 1994, Eur J Biochem 226:413-422) constitutes a new architecture for alpha-class proteins. 1H NMR and fluorescence studies show that this protein forms well-defined complexes in aqueous solution with lysophosphatidylcholine. Dissociation constants, Kd, of 1.9 +/- 0.6 x 10(-6) M and > 10(-3) M were obtained with lyso-C16 and -C12, respectively. A structure model for a lipid-protein complex is proposed in which the aliphatic chain of the phospholipid is inserted in the internal cavity and the polar head interacts with the charged side chains located at one end of this cavity. Our model for the lipid-protein complex is qualitatively very similar to the recently published crystal structure (Shin DH et al., 1995, Structure 3:189-199).
About this Structure
1AFH is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.
Reference
Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds., Gomar J, Petit MC, Sodano P, Sy D, Marion D, Kader JC, Vovelle F, Ptak M, Protein Sci. 1996 Apr;5(4):565-77. PMID:8845747
Page seeded by OCA on Thu Mar 20 09:56:48 2008
