View source for 2mk0


==Structure of the PSCD4-domain of the cell wall protein pleuralin-1 from the diatom Cylindrotheca fusiformis==
<StructureSection load='2mk0' size='340' side='right'caption='[[2mk0]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mk0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cylindrotheca_fusiformis Cylindrotheca fusiformis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MK0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=2mk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mk0 OCA], [https://pdbe.org/2mk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mk0 RCSB], [https://www.ebi.ac.uk/pdbsum/2mk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mk0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O22015_CYLFU O22015_CYLFU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Diatoms are eukaryotic unicellular algae characterized by silica cell walls and associated with three unique protein families, the pleuralins, frustulins, and silaffins. The NMR structure of the PSCD4 domain of pleuralin-1 from Cylindrotheca fusiformis contains only three short helical elements and is stabilized by five unique disulfide bridges. PSCD4 contains two binding sites for Ca(2+) ions with millimolar affinity. NMR-based interaction studies show an interaction of the domain with native silaffin-1A as well as with alpha-frustulins. The interaction sites of the two proteins mapped on the PSCD4 structure are contiguous and show only a small overlap. A plausible functional role of pleuralin could be to bind simultaneously silaffin-1A located inside the cell wall and alpha-frustulin coating the cell wall, thus connecting the interfaces between hypotheca and epitheca at the girdle bands. Restrained molecular dynamics calculations suggest a bead-chain-like structure of the central part of pleuralin-1.

PSCD Domains of Pleuralin-1 from the Diatom Cylindrotheca fusiformis: NMR Structures and Interactions with Other Biosilica-Associated Proteins.,De Sanctis S, Wenzler M, Kroger N, Malloni WM, Sumper M, Deutzmann R, Zadravec P, Brunner E, Kremer W, Kalbitzer HR Structure. 2016 Jul 6;24(7):1178-91. doi: 10.1016/j.str.2016.04.021. Epub 2016, Jun 16. PMID:27320836<ref>PMID:27320836</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mk0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cylindrotheca fusiformis]]
[[Category: Large Structures]]
[[Category: Brunner E]]
[[Category: De Sanctis S]]
[[Category: Deutzmann R]]
[[Category: Kalbitzer SHR]]
[[Category: Kremer W]]
[[Category: Kroeger N]]
[[Category: Malloni WM]]
[[Category: Sumper M]]
[[Category: Wenzler M]]
[[Category: Zadravec P]]