|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5yri' size='340' side='right'caption='[[5yri]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='5yri' size='340' side='right'caption='[[5yri]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yri]] 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=5YRI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YRI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yri]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pteria_penguin Pteria penguin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YRI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.65Å</td></tr> |
| - | <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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PRD_900006:trehalose'>PRD_900006</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yri OCA], [http://pdbe.org/5yri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yri RCSB], [http://www.ebi.ac.uk/pdbsum/5yri PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yri 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=5yri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yri OCA], [https://pdbe.org/5yri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yri RCSB], [https://www.ebi.ac.uk/pdbsum/5yri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yri ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B6F0T7_PTEPN B6F0T7_PTEPN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 25: |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Pteria penguin]] | | [[Category: Pteria penguin]] |
| - | [[Category: Nakae, S]] | + | [[Category: Nakae S]] |
| - | [[Category: Ogawa, T]] | + | [[Category: Ogawa T]] |
| - | [[Category: Shionyu, M]] | + | [[Category: Shionyu M]] |
| - | [[Category: Shirai, T]] | + | [[Category: Shirai T]] |
| - | [[Category: Biomineralization]]
| + | |
| - | [[Category: Calcite]]
| + | |
| - | [[Category: Docking simulation]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Post-translational modification]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
B6F0T7_PTEPN
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakae S, Shionyu M, Ogawa T, Shirai T. Structures of jacalin-related lectin PPL3 regulating pearl shell biomineralization. Proteins. 2018 Jun;86(6):644-653. doi: 10.1002/prot.25491. Epub 2018 Mar 23. PMID:29524263 doi:http://dx.doi.org/10.1002/prot.25491
|
