1ezg

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[[Image:1ezg.gif|left|200px]]
[[Image:1ezg.gif|left|200px]]
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{{Structure
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|PDB= 1ezg |SIZE=350|CAPTION= <scene name='initialview01'>1ezg</scene>, resolution 1.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1ezg", creates the "Structure Box" on the page.
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|SITE=
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|GENE= CDNA FROM FAT BODY LIBRARY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7067 Tenebrio molitor])
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|DOMAIN=
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{{STRUCTURE_1ezg| PDB=1ezg | SCENE= }}
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|RELATEDENTRY=[[1eww|1EWW]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ezg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ezg OCA], [http://www.ebi.ac.uk/pdbsum/1ezg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ezg RCSB]</span>
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'''CRYSTAL STRUCTURE OF ANTIFREEZE PROTEIN FROM THE BEETLE, TENEBRIO MOLITOR'''
'''CRYSTAL STRUCTURE OF ANTIFREEZE PROTEIN FROM THE BEETLE, TENEBRIO MOLITOR'''
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[[Category: Liou, Y C.]]
[[Category: Liou, Y C.]]
[[Category: Tocilj, A.]]
[[Category: Tocilj, A.]]
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[[Category: insect antifreeze protein]]
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[[Category: Insect antifreeze protein]]
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[[Category: iodination]]
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[[Category: Iodination]]
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[[Category: right-handed beta-helix]]
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[[Category: Right-handed beta-helix]]
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[[Category: tenebrio molitor]]
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[[Category: Tenebrio molitor]]
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[[Category: thermal hysteresis]]
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[[Category: Thermal hysteresis]]
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[[Category: tmafp]]
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[[Category: Tmafp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:42:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:12:47 2008''
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Revision as of 12:42, 2 May 2008

Image:1ezg.gif

Template:STRUCTURE 1ezg

CRYSTAL STRUCTURE OF ANTIFREEZE PROTEIN FROM THE BEETLE, TENEBRIO MOLITOR


Overview

Insect antifreeze proteins (AFP) are much more effective than fish AFPs at depressing solution freezing points by ice-growth inhibition. AFP from the beetle Tenebrio molitor is a small protein (8.4 kDa) composed of tandem 12-residue repeats (TCTxSxxCxxAx). Here we report its 1.4-A resolution crystal structure, showing that this repetitive sequence translates into an exceptionally regular beta-helix. Not only are the 12-amino-acid loops almost identical in the backbone, but also the conserved side chains are positioned in essentially identical orientations, making this AFP perhaps the most regular protein structure yet observed. The protein has almost no hydrophobic core but is stabilized by numerous disulphide and hydrogen bonds. On the conserved side of the protein, threonine-cysteine-threonine motifs are arrayed to form a flat beta-sheet, the putative ice-binding surface. The threonine side chains have exactly the same rotameric conformation and the spacing between OH groups is a near-perfect match to the ice lattice. Together with tightly bound co-planar external water, three ranks of oxygen atoms form a two-dimensional array, mimicking an ice section.

About this Structure

1EZG is a Single protein structure of sequence from Tenebrio molitor. Full crystallographic information is available from OCA.

Reference

Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein., Liou YC, Tocilj A, Davies PL, Jia Z, Nature. 2000 Jul 20;406(6793):322-4. PMID:10917536 Page seeded by OCA on Fri May 2 15:42:22 2008

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