1ops: Difference between revisions

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<StructureSection load='1ops' size='340' side='right'caption='[[1ops]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1ops' size='340' side='right'caption='[[1ops]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ops]] is a 1 chain structure with 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=1OPS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OPS FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ops]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zoarces_americanus Zoarces americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPS FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ops FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ops OCA], [http://pdbe.org/1ops PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ops RCSB], [http://www.ebi.ac.uk/pdbsum/1ops PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ops ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=1ops FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ops OCA], [https://pdbe.org/1ops PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ops RCSB], [https://www.ebi.ac.uk/pdbsum/1ops PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ops ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ANP1_ZOAAM ANP1_ZOAAM]] Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth (By similarity).  
[https://www.uniprot.org/uniprot/ANP1_ZOAAM ANP1_ZOAAM] Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1ops ConSurf].
</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=1ops ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antifreeze proteins (AFPs) adsorb to surfaces of growing ice crystals, thereby arresting their growth. The prevailing hypothesis explains the nature of adsorption in terms of a match between the hydrophilic side chains on the AFP's ice-binding surface (IBS) and the water molecules on the ice surface. The number and spatial arrangement of hydrogen bonds thus formed have been proposed to account, respectively, for the binding affinity and specificity. The crystal structure of a type III AFP from ocean pout (isoform HPLC-3) has been determined to 2.0-A resolution. The structure reveals an internal dyad motif formed by two 19-residue, loop-shaped elements. Based on of the flatness observed on the type I alpha-helical AFP's IBS, an automated algorithm was developed to analyze the surface planarity of the globular type III AFP and was used to identify the IBS on this protein. The surface with the highest flatness score is formed by one loop of the dyad motif and is identical to the IBS deduced from earlier mutagenesis studies. Interestingly, 67% of this surface contains nonpolar solvent-accessible surface area. The success of our approach to identifying the IBS on an AFP, without considering the presence of polar side chains, indicates that flatness is the first approximation of an IBS. We further propose that the specificity of interactions between an IBS and a particular ice-crystallographic plane arises from surface complementarity.
Identification of the ice-binding surface on a type III antifreeze protein with a "flatness function" algorithm.,Yang DS, Hon WC, Bubanko S, Xue Y, Seetharaman J, Hew CL, Sicheri F Biophys J. 1998 May;74(5):2142-51. PMID:9591641<ref>PMID:9591641</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ops" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Macrozoarces americanus]]
[[Category: Zoarces americanus]]
[[Category: Bubanko, S]]
[[Category: Bubanko S]]
[[Category: Hew, C L]]
[[Category: Hew CL]]
[[Category: Hon, W C]]
[[Category: Hon W-C]]
[[Category: Seetharaman, J]]
[[Category: Seetharaman J]]
[[Category: Sicheri, F]]
[[Category: Sicheri F]]
[[Category: Xue, Y]]
[[Category: Xue Y]]
[[Category: Yang, D S.C]]
[[Category: Yang DSC]]
[[Category: Antifreeze protein]]
[[Category: Glycoprotein]]
[[Category: Ice crystal growth inhibition]]
[[Category: Pretzel fold]]

Latest revision as of 11:02, 14 February 2024

ICE-BINDING SURFACE ON A TYPE III ANTIFREEZE PROTEIN FROM OCEAN POUTICE-BINDING SURFACE ON A TYPE III ANTIFREEZE PROTEIN FROM OCEAN POUT

Structural highlights

1ops is a 1 chain structure with sequence from Zoarces americanus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ANP1_ZOAAM Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ops, resolution 2.00Å

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