5yrg

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'''Unreleased structure'''
 
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The entry 5yrg is ON HOLD until Paper Publication
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==PPL3A-isomaltose complex==
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<StructureSection load='5yrg' size='340' side='right' caption='[[5yrg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5yrg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pteria_penguin Pteria penguin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YRG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YRG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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<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=5yrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yrg OCA], [http://pdbe.org/5yrg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yrg RCSB], [http://www.ebi.ac.uk/pdbsum/5yrg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yrg ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The nacreous layer of pearl oysters is one of the major biominerals of commercial and industrial interest. Jacalin-related lectins, including PPL3 isoforms, are known to regulate biomineralization of the Pteria penguin pearl shell, although the molecular mechanisms are largely unknown. The PPL3 crystal structures were determined partly by utilizing microgravity environments for 3 isoforms, namely, PPL3A, PPL3B, and PPL3C. The structures revealed a tail-to-tail dimer structure established by forming a unique inter-subunit disulfide bond at C-termini. The N-terminal residues were found in pyroglutamate form, and this was partly explained by the post-translational modification of PPL3 isoforms implied from the discrepancy between amino acid and gene sequences. The complex structures with trehalose and isomaltose indicated that the novel specificity originated from the unique alpha-helix of PPL3 isoforms. Docking simulations of PPL3B to various calcite crystal faces suggested the edge of a beta-sheet and the carbohydrate-binding site rich in charged residues were the interface to the biomineral, and implied that the isoforms differed in calcite interactions.
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Authors: Nakae, S., Shionyu, M., Ogawa, T., Shirai, T.
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Structures of jacalin-related lectin PPL3 regulating pearl shell biomineralization.,Nakae S, Shionyu M, Ogawa T, Shirai T Proteins. 2018 Jun;86(6):644-653. doi: 10.1002/prot.25491. Epub 2018 Mar 23. PMID:29524263<ref>PMID:29524263</ref>
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Description: PPL3A-isomaltose complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Shionyu, M]]
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<div class="pdbe-citations 5yrg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Pteria penguin]]
[[Category: Nakae, S]]
[[Category: Nakae, S]]
[[Category: Ogawa, T]]
[[Category: Ogawa, T]]
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[[Category: Shionyu, M]]
[[Category: Shirai, T]]
[[Category: Shirai, T]]
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[[Category: Biomineralization]]
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[[Category: Calcite]]
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[[Category: Docking simulation]]
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[[Category: Lectin]]
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[[Category: Post-translational modification]]
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[[Category: Sugar binding protein]]

Revision as of 07:19, 29 August 2018

PPL3A-isomaltose complex

5yrg, resolution 1.50Å

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