1mzm
From Proteopedia
(New page: 200px<br /><applet load="1mzm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mzm, resolution 1.78Å" /> '''MAIZE NONSPECIFIC LI...) |
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| - | [[Image:1mzm.jpg|left|200px]]<br /><applet load="1mzm" size=" | + | [[Image:1mzm.jpg|left|200px]]<br /><applet load="1mzm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mzm, resolution 1.78Å" /> | caption="1mzm, resolution 1.78Å" /> | ||
'''MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE'''<br /> | '''MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The movement of lipids between membranes is aided by | + | 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== | ==About this Structure== | ||
| - | 1MZM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with PLM and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MZM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=PLM:'>PLM</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
| - | [[Category: Lee, J | + | [[Category: Lee, J Y.]] |
| - | [[Category: Shin, D | + | [[Category: Shin, D H.]] |
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
[[Category: FMT]] | [[Category: FMT]] | ||
[[Category: PLM]] | [[Category: PLM]] | ||
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[[Category: lipid transport]] | [[Category: lipid transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:51 2008'' |
Revision as of 12:00, 21 February 2008
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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 with and as ligands. 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 Feb 21 14:00:51 2008
Categories: Single protein | Zea mays | Lee, J Y. | Shin, D H. | Suh, S W. | FMT | PLM | Alpha-helical structure | Lipid transport
