4uxm
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4uxm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Struthio_camelus Struthio camelus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UXM FirstGlance]. <br> | <table><tr><td colspan='2'>[[4uxm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Struthio_camelus Struthio camelus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UXM FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BE7:(4-CARBOXYPHENYL)(CHLORO)MERCURY'>BE7</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]] 1.5Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BE7:(4-CARBOXYPHENYL)(CHLORO)MERCURY'>BE7</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=4uxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uxm OCA], [https://pdbe.org/4uxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uxm RCSB], [https://www.ebi.ac.uk/pdbsum/4uxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uxm 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=4uxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uxm OCA], [https://pdbe.org/4uxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uxm RCSB], [https://www.ebi.ac.uk/pdbsum/4uxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uxm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SCAL1_STRCA SCAL1_STRCA] | [https://www.uniprot.org/uniprot/SCAL1_STRCA SCAL1_STRCA] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Biomineralization is the process by which living organisms produce minerals. One remarkable example is the formation of eggshells in birds. Struthiocalcins present in the ostrich (Struthio camellus) eggshell matrix act as biosensors of calcite growth during eggshell formation. Here, the crystal structure of struthiocalcin-1 (SCA-1) is reported in two different crystal forms. The structure is a compact single domain with an alpha/beta fold characteristic of the C-type lectin family. In contrast to the related avian ovocleidin OC17, the electrostatic potential on the molecular surface is dominated by an acidic patch. Scanning electron microscopy combined with Raman spectroscopy indicates that these intramineral proteins (SCA-1 and SCA-2) induce calcium carbonate precipitation, leading to the formation of a stable form of calcite in the mature eggshell. Finally, the implications of these two intramineral proteins SCA-1 and SCA-2 in the nucleation of calcite during the formation of eggshells in ratite birds are discussed. | ||
| - | |||
| - | Structure of struthiocalcin-1, an intramineral protein from Struthio camelus eggshell, in two crystal forms.,Ruiz-Arellano RR, Medrano FJ, Moreno A, Romero A Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):809-18. doi:, 10.1107/S139900471500125X. Epub 2015 Mar 26. PMID:25849392<ref>PMID:25849392</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4uxm" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 12:58, 1 March 2024
Crystal Structure of Struthiocalcin-1, a different crystal form.
| |||||||||||
