2py2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2py2.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2py2", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2py2|  PDB=2py2  |  SCENE=  }}
'''Structure of Herring Type II Antifreeze Protein'''


==Structure of Herring Type II Antifreeze Protein==
<StructureSection load='2py2' size='340' side='right'caption='[[2py2]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2py2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Clupea_harengus Clupea harengus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PY2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2py2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py2 OCA], [https://pdbe.org/2py2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2py2 RCSB], [https://www.ebi.ac.uk/pdbsum/2py2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2py2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q91992_CLUHA Q91992_CLUHA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/py/2py2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2py2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:17579720</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2PY2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clupea_harengus Clupea harengus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY2 OCA].
</div>
<div class="pdbe-citations 2py2" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17579720 17579720]
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clupea harengus]]
[[Category: Clupea harengus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hew, C L.]]
[[Category: Hew C-L]]
[[Category: Li, Z.]]
[[Category: Li Z]]
[[Category: Lin, Q.]]
[[Category: Lin Q]]
[[Category: Liu, Y.]]
[[Category: Liu Y]]
[[Category: Seetharaman, J.]]
[[Category: Seetharaman J]]
[[Category: Sivaraman, J.]]
[[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''

Latest revision as of 01:20, 21 November 2024

Structure of Herring Type II Antifreeze Protein

2py2, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2py2&oldid=4270803"