1mzm
From Proteopedia
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'''MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE''' | '''MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE''' | ||
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[[Category: Shin, D H.]] | [[Category: Shin, D H.]] | ||
[[Category: Suh, S W.]] | [[Category: Suh, S W.]] | ||
| - | [[Category: | + | [[Category: Alpha-helical structure]] |
| - | [[Category: | + | [[Category: Lipid transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:54:30 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:54, 2 May 2008
MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE
Overview
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 have determined the crystal structure of ns-LTP from maize seedlings by multiple isomorphous replacement and refined the structure to 1.9 A resolution. The protein comprises a single compact domain with four alpha-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 A 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 to accommodate a long fatty acyl chain. In the structure of the complex with palmitate, most of the acyl chain is buried inside this hydrophobic cavity.
About this Structure
1MZM is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.
Reference
High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings., Shin DH, Lee JY, Hwang KY, Kim KK, Suh SW, Structure. 1995 Feb 15;3(2):189-99. PMID:7735835 Page seeded by OCA on Sat May 3 01:54:30 2008
