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1kde

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{{STRUCTURE_1kde| PDB=1kde | SCENE= }}
{{STRUCTURE_1kde| PDB=1kde | SCENE= }}
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'''NORTH-ATLANTIC OCEAN POUT ANTIFREEZE PROTEIN TYPE III ISOFORM HPLC12 MUTANT, NMR, 22 STRUCTURES'''
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===NORTH-ATLANTIC OCEAN POUT ANTIFREEZE PROTEIN TYPE III ISOFORM HPLC12 MUTANT, NMR, 22 STRUCTURES===
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==Overview==
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BACKGROUND: Antifreeze proteins are found in certain fish inhabiting polar sea water. These proteins depress the freezing points of blood and body fluids below that of the surrounding sea water by binding to and inhibiting the growth of seed ice crystals. The proteins are believed to bind irreversibly to growing ice crystals in such a way as to change the curvature of the ice-water interface, leading to freezing point depression, but the mechanism of high-affinity ice binding is not yet fully understood. RESULTS: The solution structure of the type III antifreeze protein was determined by multidimensional NMR spectroscopy. Twenty-two structures converged and display a root mean square difference from the mean of 0.26 A for backbone atoms and 0.62 A for all non-hydrogen atoms. The protein exhibits a compact fold with a relatively large hydrophobic core, several short and irregular beta sheets and one helical turn. The ice-binding site, which encompasses parts of the C-terminal sheet and a loop, is planar and relatively nonpolar. The site is further characterized by the low solvent accessibilities and the specific spatial arrangement of the polar side-chain atoms of the putative ice-binding residues Gln9, Asn14, Thr15, Thr18 and Gln44. CONCLUSIONS: In agreement with the adsorption-inhibition mechanism of action, interatomic distances between active polar protein residues match the spacing of water molecules in the prism planes ( inverted question mark10&1macr;0 inverted question mark) of the hexagonal ice crystal. The particular side-chain conformations, however, limit the number and strength of possible proten-ice hydrogen bonds. This suggests that other entropic and enthalpic contributions, such as those arising from hydrophobic groups, could play a role in the high-affinity protein-ice adsorption.
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{{ABSTRACT_PUBMED_8939756}}
==About this Structure==
==About this Structure==
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1KDE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Macrozoarces_americanus Macrozoarces americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDE OCA].
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1KDE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Macrozoarces_americanus Macrozoarces americanus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDE OCA].
==Reference==
==Reference==
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[[Category: Ice binding protein]]
[[Category: Ice binding protein]]
[[Category: Thermal hysteresis protein]]
[[Category: Thermal hysteresis protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:10:00 2008''

Revision as of 07:10, 2 July 2008

Image:1kde.png

Template:STRUCTURE 1kde

NORTH-ATLANTIC OCEAN POUT ANTIFREEZE PROTEIN TYPE III ISOFORM HPLC12 MUTANT, NMR, 22 STRUCTURES

Template:ABSTRACT PUBMED 8939756

About this Structure

1KDE is a Single protein structure of sequence from Macrozoarces americanus. Full experimental information is available from OCA.

Reference

Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction., Sonnichsen FD, DeLuca CI, Davies PL, Sykes BD, Structure. 1996 Nov 15;4(11):1325-37. PMID:8939756

Page seeded by OCA on Wed Jul 2 10:10:00 2008

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