3nla

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:46, 22 May 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3nla.jpg|left|200px]]<br /><applet load="3nla" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="3nla" />
 
-
'''NMR STRUCTURE OF THE N-TERMINAL DOMAIN WITH A LINKER PORTION OF ANTARCTIC EEL POUT ANTIFREEZE PROTEIN RD3, 40 STRUCTURES'''<br />
 
-
==Overview==
+
==NMR STRUCTURE OF THE N-TERMINAL DOMAIN WITH A LINKER PORTION OF ANTARCTIC EEL POUT ANTIFREEZE PROTEIN RD3, 40 STRUCTURES==
-
Antifreeze proteins (AFPs) have the unique ability to adsorb to ice and, inhibit its growth. Many organisms ranging from fish to bacteria use AFPs, to retard freezing or lessen the damage incurred upon freezing and, thawing. The ice-binding mechanism of the long linear alpha-helical type I, AFPs has been attributed to their regularly spaced polar residues matching, the ice lattice along a pyramidal plane. In contrast, it is not known how, globular antifreeze proteins such as type III AFP that lack repeating, ice-binding residues bind to ice. Here we report the 1.25 A crystal, structure of recombinant type III AFP (QAE isoform) from eel pout, (Macrozoarces americanus), which reveals a remarkably flat amphipathic, ice-binding site where five hydrogen-bonding atoms match two ranks of, oxygens on the [1010] ice prism plane in the &lt;0001&gt; direction, giving high, ice-binding affinity and specificity. This binding site, substantiated by, the structures and properties of several ice-binding site mutants, suggests that the AFP occupies a niche in the ice surface in which it, covers the basal plane while binding to the prism face.
+
<StructureSection load='3nla' size='340' side='right'caption='[[3nla]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3nla]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lycodichthys_dearborni Lycodichthys dearborni]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NLA FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=3nla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nla OCA], [https://pdbe.org/3nla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nla RCSB], [https://www.ebi.ac.uk/pdbsum/3nla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nla ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ANP3_LYCDA ANP3_LYCDA] 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 ==
 +
[[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/nl/3nla_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3nla ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Antifreeze proteins (AFPs) have the unique ability to adsorb to ice and inhibit its growth. Many organisms ranging from fish to bacteria use AFPs to retard freezing or lessen the damage incurred upon freezing and thawing. The ice-binding mechanism of the long linear alpha-helical type I AFPs has been attributed to their regularly spaced polar residues matching the ice lattice along a pyramidal plane. In contrast, it is not known how globular antifreeze proteins such as type III AFP that lack repeating ice-binding residues bind to ice. Here we report the 1.25 A crystal structure of recombinant type III AFP (QAE isoform) from eel pout (Macrozoarces americanus), which reveals a remarkably flat amphipathic ice-binding site where five hydrogen-bonding atoms match two ranks of oxygens on the [1010] ice prism plane in the &lt;0001&gt; direction, giving high ice-binding affinity and specificity. This binding site, substantiated by the structures and properties of several ice-binding site mutants, suggests that the AFP occupies a niche in the ice surface in which it covers the basal plane while binding to the prism face.
-
==About this Structure==
+
Structural basis for the binding of a globular antifreeze protein to ice.,Jia Z, DeLuca CI, Chao H, Davies PL Nature. 1996 Nov 21;384(6606):285-8. PMID:8918883<ref>PMID:8918883</ref>
-
3NLA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lycodichthys_dearborni Lycodichthys dearborni]. Known structural/functional Site: <scene name='pdbsite=1:Ice+Binding+Site'>1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NLA OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Structural basis for the binding of a globular antifreeze protein to ice., Jia Z, DeLuca CI, Chao H, Davies PL, Nature. 1996 Nov 21;384(6606):285-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8918883 8918883]
+
</div>
-
[[Category: Lycodichthys dearborni]]
+
<div class="pdbe-citations 3nla" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Hikichi, K.]]
+
-
[[Category: Hoshino, T.]]
+
-
[[Category: Miura, K.]]
+
-
[[Category: Nemoto, N.]]
+
-
[[Category: Ohgiya, S.]]
+
-
[[Category: Tsuda, S.]]
+
-
[[Category: antifreeze protein]]
+
-
[[Category: ice binding protein]]
+
-
[[Category: thermal hysteresis protein]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:52:05 2008''
+
==See Also==
 +
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Lycodichthys dearborni]]
 +
[[Category: Hikichi K]]
 +
[[Category: Hoshino T]]
 +
[[Category: Miura K]]
 +
[[Category: Nemoto N]]
 +
[[Category: Ohgiya S]]
 +
[[Category: Tsuda S]]

Current revision

NMR STRUCTURE OF THE N-TERMINAL DOMAIN WITH A LINKER PORTION OF ANTARCTIC EEL POUT ANTIFREEZE PROTEIN RD3, 40 STRUCTURES

PDB ID 3nla

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools