View source for 2mx8


==NMR structure of N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 7.2==
<StructureSection load='2mx8' size='340' side='right'caption='[[2mx8]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mx8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Araneus_ventricosus Araneus ventricosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MX8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=2mx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mx8 OCA], [https://pdbe.org/2mx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mx8 RCSB], [https://www.ebi.ac.uk/pdbsum/2mx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mx8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K4MTL7_ARAVE K4MTL7_ARAVE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Conversion of spider silk proteins from soluble dope to insoluble fibers involves pH-dependent dimerization of the N-terminal domain (NT). This conversion is tightly regulated to prevent premature precipitation and enable rapid silk formation at the end of the duct. Three glutamic acid residues that mediate this process in the NT from Euprosthenops australis major ampullate spidroin 1 are well conserved among spidroins. However, NTs of minor ampullate spidroins from several species, including Araneus ventricosus ((Av) MiSp NT), lack one of the glutamic acids. Here we investigate the pH-dependent structural changes of (Av) MiSp NT, revealing that it uses the same mechanism but involves a non-conserved glutamic acid residue instead. Homology modeling of the structures of other MiSp NTs suggests that these harbor different compensatory residues. This indicates that, despite sequence variations, the molecular mechanism underlying pH-dependent dimerization of NT is conserved among different silk types.

Diversified Structural Basis of a Conserved Molecular Mechanism for pH-Dependent Dimerization in Spider Silk N-Terminal Domains.,Otikovs M, Chen G, Nordling K, Landreh M, Meng Q, Jornvall H, Kronqvist N, Rising A, Johansson J, Jaudzems K Chembiochem. 2015 Aug 17;16(12):1720-4. doi: 10.1002/cbic.201500263. Epub 2015, Jul 1. PMID:26033527<ref>PMID:26033527</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mx8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Araneus ventricosus]]
[[Category: Large Structures]]
[[Category: Chen G]]
[[Category: Jaudzems K]]
[[Category: Johansson J]]
[[Category: Nordling K]]
[[Category: Otikovs M]]
[[Category: Rising A]]