1ucs

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(New page: 200px<br /><applet load="1ucs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ucs, resolution 0.62&Aring;" /> '''Type III Antifreeze ...)
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'''Type III Antifreeze Protein RD1 from an Antarctic Eel Pout'''<br />
'''Type III Antifreeze Protein RD1 from an Antarctic Eel Pout'''<br />
==Overview==
==Overview==
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RD1 is a 7-kDa globular protein from the Antarctic eel pout Lycodichthys, dearborni. It belongs to type III of the four types of antifreeze proteins, (AFPs) found in marine fishes living at subzero temperatures. For type III, AFP, a potential ice-binding flat surface has been identified and is, imbedded with side chains capable of making hydrogen bonds with a specific, lattice plane on ice. So far, all crystallographic studies on type III, AFPs were carried out using the Atlantic ocean pout Macrozoarces, americanus as the source organism. Here we present the crystal structure, of a type III AFP from a different zoarcid fish, and at an ultra-high, resolution of 0.62 A. The protein fold of RD1 comprises a compact globular, domain with two internal tandem motifs arranged about a pseudo-dyad, symmetry. Each motif of the "pretzel fold" includes four short, beta-strands and a 3(10) helix. There is a novel internal cavity of 45, A(3) surrounded by eight conserved nonpolar residues. The model contains, several residues with alternate conformations, and a number of split water, molecules, probably caused by alternate interactions with the protein, molecule. After extensive refinement that includes hydrogen atoms, significant residual electron densities associated with the electrons of, peptides and many other bonds could be visualized.
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RD1 is a 7-kDa globular protein from the Antarctic eel pout Lycodichthys dearborni. It belongs to type III of the four types of antifreeze proteins (AFPs) found in marine fishes living at subzero temperatures. For type III AFP, a potential ice-binding flat surface has been identified and is imbedded with side chains capable of making hydrogen bonds with a specific lattice plane on ice. So far, all crystallographic studies on type III AFPs were carried out using the Atlantic ocean pout Macrozoarces americanus as the source organism. Here we present the crystal structure of a type III AFP from a different zoarcid fish, and at an ultra-high resolution of 0.62 A. The protein fold of RD1 comprises a compact globular domain with two internal tandem motifs arranged about a pseudo-dyad symmetry. Each motif of the "pretzel fold" includes four short beta-strands and a 3(10) helix. There is a novel internal cavity of 45 A(3) surrounded by eight conserved nonpolar residues. The model contains several residues with alternate conformations, and a number of split water molecules, probably caused by alternate interactions with the protein molecule. After extensive refinement that includes hydrogen atoms, significant residual electron densities associated with the electrons of peptides and many other bonds could be visualized.
==About this Structure==
==About this Structure==
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1UCS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lycodichthys_dearborni Lycodichthys dearborni]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UCS OCA].
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1UCS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lycodichthys_dearborni Lycodichthys dearborni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCS OCA].
==Reference==
==Reference==
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[[Category: Lycodichthys dearborni]]
[[Category: Lycodichthys dearborni]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cheng, C.H.C.]]
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[[Category: Cheng, C H.C.]]
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[[Category: DeVries, A.L.]]
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[[Category: DeVries, A L.]]
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[[Category: Gao, Y.G.]]
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[[Category: Gao, Y G.]]
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[[Category: Ko, T.P.]]
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[[Category: Ko, T P.]]
[[Category: Robinson, H.]]
[[Category: Robinson, H.]]
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[[Category: Wang, A.H.J.]]
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[[Category: Wang, A H.J.]]
[[Category: pretzel fold]]
[[Category: pretzel fold]]
[[Category: small beta barrel]]
[[Category: small beta barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:05 2008''

Revision as of 13:23, 21 February 2008


1ucs, resolution 0.62Å

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Type III Antifreeze Protein RD1 from an Antarctic Eel Pout

Overview

RD1 is a 7-kDa globular protein from the Antarctic eel pout Lycodichthys dearborni. It belongs to type III of the four types of antifreeze proteins (AFPs) found in marine fishes living at subzero temperatures. For type III AFP, a potential ice-binding flat surface has been identified and is imbedded with side chains capable of making hydrogen bonds with a specific lattice plane on ice. So far, all crystallographic studies on type III AFPs were carried out using the Atlantic ocean pout Macrozoarces americanus as the source organism. Here we present the crystal structure of a type III AFP from a different zoarcid fish, and at an ultra-high resolution of 0.62 A. The protein fold of RD1 comprises a compact globular domain with two internal tandem motifs arranged about a pseudo-dyad symmetry. Each motif of the "pretzel fold" includes four short beta-strands and a 3(10) helix. There is a novel internal cavity of 45 A(3) surrounded by eight conserved nonpolar residues. The model contains several residues with alternate conformations, and a number of split water molecules, probably caused by alternate interactions with the protein molecule. After extensive refinement that includes hydrogen atoms, significant residual electron densities associated with the electrons of peptides and many other bonds could be visualized.

About this Structure

1UCS is a Single protein structure of sequence from Lycodichthys dearborni. Full crystallographic information is available from OCA.

Reference

The refined crystal structure of an eel pout type III antifreeze protein RD1 at 0.62-A resolution reveals structural microheterogeneity of protein and solvation., Ko TP, Robinson H, Gao YG, Cheng CH, DeVries AL, Wang AH, Biophys J. 2003 Feb;84(2 Pt 1):1228-37. PMID:12547803

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