1mzl
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1mzl.jpg|left|200px]] | + | [[Image:1mzl.jpg|left|200px]] |
| - | + | ||
| - | '''MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN''' | + | {{Structure |
| + | |PDB= 1mzl |SIZE=350|CAPTION= <scene name='initialview01'>1mzl</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1MZL is a [ | + | 1MZL 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=1MZL OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7735835 7735835] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
| Line 21: | Line 30: | ||
[[Category: lipid transport]] | [[Category: lipid transport]] | ||
| - | ''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 12:50:11 2008'' |
Revision as of 10:50, 20 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN
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
1MZL 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 Thu Mar 20 12:50:11 2008
