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Literature DB >> 8438165

The nonhelical structure of antifreeze protein type III.

F D Sönnichsen¹, B D Sykes, H Chao, P L Davies.

Abstract

Antifreeze proteins (AFPs) are present in the blood of some marine fishes and inhibit the growth of ice crystals at subzero temperatures by adsorption to the ice lattice. The solution structure of a Type III AFP was determined by two-dimensional nuclear magnetic resonance spectroscopy. These measurements indicate that this 66-residue protein has an unusual fold in which eight beta strands form two sheets of three antiparallel strands and one sheet of two antiparallel strands, and the triple-stranded sheets are packed orthogonally into a beta sandwich. This structure is completely different from the amphipathic, helical structure observed for Type I AFPs.

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Year: 1993 PMID： 8438165 DOI： 10.1126/science.8438165

Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728

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Cited

21 in total

1. Structure and interactions of fish type III antifreeze protein in solution.

Authors: Andrés G Salvay; Frank Gabel; Bernard Pucci; Javier Santos; Eduardo I Howard; Christine Ebel
Journal: Biophys J Date: 2010-07-21 Impact factor: 4.033

2. Increased flexibility decreases antifreeze protein activity.

Authors: Shruti N Patel; Steffen P Graether
Journal: Protein Sci Date: 2010-11-11 Impact factor: 6.725

3. Crystallization and preliminary X-ray crystallographic analysis of Ca2+-independent and Ca2+-dependent species of the type II antifreeze protein.

Authors: Yoshiyuki Nishimiya; Hidemasa Kondo; Masanori Yasui; Hiroshi Sugimoto; Natsuko Noro; Ryoko Sato; Mamoru Suzuki; Ai Miura; Sakae Tsuda
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2006-05-31

The nonhelical structure of antifreeze protein type III.

1. Structure and interactions of fish type III antifreeze protein in solution.

2. Increased flexibility decreases antifreeze protein activity.

3. Crystallization and preliminary X-ray crystallographic analysis of Ca2+-independent and Ca2+-dependent species of the type II antifreeze protein.

4. Activity of a two-domain antifreeze protein is not dependent on linker sequence.

5. Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation.

6. Comparative modeling of the three-dimensional structure of type II antifreeze protein.

7. Effect of type III antifreeze protein dilution and mutation on the growth inhibition of ice.

8. Extraction and Isolation of Antifreeze Proteins from Winter Rye (Secale cereale L.) Leaves.

9. Crystallization and preliminary X-ray crystallographic studies on Type III antifreeze protein.

10. Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein.