3p4g

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Current revision (10:38, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3p4g' size='340' side='right'caption='[[3p4g]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3p4g' size='340' side='right'caption='[[3p4g]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3p4g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Jcm_11775 Jcm 11775]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P4G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3p4g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinomonas_primoryensis Marinomonas primoryensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P4G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MpAFP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178399 JCM 11775])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3p4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p4g OCA], [https://pdbe.org/3p4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p4g RCSB], [https://www.ebi.ac.uk/pdbsum/3p4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p4g ProSAT]</span></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=3p4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p4g OCA], [https://pdbe.org/3p4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p4g RCSB], [https://www.ebi.ac.uk/pdbsum/3p4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p4g ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A1YIY3_9GAMM A1YIY3_9GAMM]
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The mechanism by which antifreeze proteins (AFPs) irreversibly bind to ice has not yet been resolved. The ice-binding site of an AFP is relatively hydrophobic, but also contains many potential hydrogen bond donors/acceptors. The extent to which hydrogen bonding and the hydrophobic effect contribute to ice binding has been debated for over 30 years. Here we have elucidated the ice-binding mechanism through solving the first crystal structure of an Antarctic bacterial AFP. This 34-kDa domain, the largest AFP structure determined to date, folds as a Ca(2+)-bound parallel beta-helix with an extensive array of ice-like surface waters that are anchored via hydrogen bonds directly to the polypeptide backbone and adjacent side chains. These bound waters make an excellent three-dimensional match to both the primary prism and basal planes of ice and in effect provide an extensive X-ray crystallographic picture of the AFPice interaction. This unobstructed view, free from crystal-packing artefacts, shows the contributions of both the hydrophobic effect and hydrogen bonding during AFP adsorption to ice. We term this mode of binding the "anchored clathrate" mechanism of AFP action.
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Anchored clathrate waters bind antifreeze proteins to ice.,Garnham CP, Campbell RL, Davies PL Proc Natl Acad Sci U S A. 2011 Apr 11. PMID:21482800<ref>PMID:21482800</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3p4g" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Jcm 11775]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Campbell, R L]]
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[[Category: Marinomonas primoryensis]]
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[[Category: Davies, P L]]
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[[Category: Campbell RL]]
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[[Category: Garnham, C P]]
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[[Category: Davies PL]]
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[[Category: Antifreeze protein]]
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[[Category: Garnham CP]]
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[[Category: Right-handed ca2+-binding beta-helix]]
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Current revision

X-ray crystal structure of a hyperactive, Ca2+-dependent, beta-helical antifreeze protein from an Antarctic bacterium

PDB ID 3p4g

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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