2py2: Difference between revisions

Revision as of 02:32, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2py2.png

Template:STRUCTURE 2py2

Structure of Herring Type II Antifreeze ProteinStructure of Herring Type II Antifreeze Protein

Template:ABSTRACT PUBMED 17579720

About this StructureAbout this Structure

2PY2 is a Single protein structure of sequence from Clupea harengus. Full crystallographic information is available from OCA.

ReferenceReference

Structure and evolutionary origin of Ca2+-dependent herring type II antifreeze protein., Liu Y, Li Z, Lin Q, Kosinski J, Seetharaman J, Bujnicki JM, Sivaraman J, Hew CL, PLoS ONE. 2007 Jun 20;2(6):e548. PMID:17579720

Page seeded by OCA on Mon Jul 28 02:32:06 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2py2.gif|left|200px]]
+{{Seed}}
+[[Image:2py2.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2py2|  PDB=2py2  |  SCENE=  }}
-'''Structure of Herring Type II Antifreeze Protein'''
+===Structure of Herring Type II Antifreeze Protein===
-==Overview==
+<!--
-In order to survive under extremely cold environments, many organisms produce antifreeze proteins (AFPs). AFPs inhibit the growth of ice crystals and protect organisms from freezing damage. Fish AFPs can be classified into five distinct types based on their structures. Here we report the structure of herring AFP (hAFP), a Ca(2+)-dependent fish type II AFP. It exhibits a fold similar to the C-type (Ca(2+)-dependent) lectins with unique ice-binding features. The 1.7 A crystal structure of hAFP with bound Ca(2+) and site-directed mutagenesis reveal an ice-binding site consisting of Thr96, Thr98 and Ca(2+)-coordinating residues Asp94 and Glu99, which initiate hAFP adsorption onto the [10-10] prism plane of the ice lattice. The hAFP-ice interaction is further strengthened by the bound Ca(2+) through the coordination with a water molecule of the ice lattice. This Ca(2+)-coordinated ice-binding mechanism is distinct from previously proposed mechanisms for other AFPs. However, phylogenetic analysis suggests that all type II AFPs evolved from the common ancestor and developed different ice-binding modes. We clarify the evolutionary relationship of type II AFPs to sugar-binding lectins.
+The line below this paragraph, {{ABSTRACT_PUBMED_17579720}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17579720 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17579720}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Sivaraman, J.]]
 [[Category: Type ii antifreeze protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 14:00:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:32:06 2008''