6r9d: Difference between revisions
New page: '''Unreleased structure''' The entry 6r9d is ON HOLD Authors: Knight, S.D., Jiang, W., Askarieh, G. Description: Crystal structure of an asymmetric dimer of the N-terminal domain of Eu... |
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The | ==Crystal structure of an asymmetric dimer of the N-terminal domain of Euprosthenops australis Major Ampullate Spidroin 1 (dragline silk)== | ||
<StructureSection load='6r9d' size='340' side='right'caption='[[6r9d]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6r9d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Euprosthenops_australis Euprosthenops australis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R9D FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=6r9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r9d OCA], [https://pdbe.org/6r9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r9d RCSB], [https://www.ebi.ac.uk/pdbsum/6r9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r9d ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q05H60_9ARAC Q05H60_9ARAC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Spider silk is a biomaterial with exceptional mechanical toughness, and there is great interest in developing biomimetic methods to produce engineered spider silk-based materials. However, the mechanisms that regulate the conversion of spider silk proteins (spidroins) from highly soluble dope into silk are not completely understood. The N-terminal domain (NT) of Euprosthenops australis dragline silk protein undergoes conformational and quaternary-structure changes from a monomer at a pH above 7 to a homodimer at lower pH values. Conversion from the monomer to the dimer requires the protonation of three conserved glutamic acid residues, resulting in a low-pH `locked' dimer stabilized by symmetric electrostatic interactions at the poles of the dimer. The detailed molecular events during this transition are still unresolved. Here, a 2.1 A resolution crystal structure of an NT T61A mutant in an alternative, asymmetric, dimer form in which the electrostatic interactions at one of the poles are dramatically different from those in symmetrical dimers is presented. A similar asymmetric dimer structure from dragline silk of Nephila clavipes has previously been described. It is suggested that asymmetric dimers represent a conserved intermediate state in spider silk formation, and a revised `lock-and-trigger' mechanism for spider silk formation is presented. | |||
Structure of the N-terminal domain of Euprosthenops australis dragline silk suggests that conversion of spidroin dope to spider silk involves a conserved asymmetric dimer intermediate.,Jiang W, Askarieh G, Shkumatov A, Hedhammar M, Knight SD Acta Crystallogr D Struct Biol. 2019 Jul 1;75(Pt 7):618-627. doi:, 10.1107/S2059798319007253. Epub 2019 Jun 26. PMID:31282471<ref>PMID:31282471</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6r9d" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Knight | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Euprosthenops australis]] | |||
[[Category: Large Structures]] | |||
[[Category: Askarieh G]] | |||
[[Category: Jiang W]] | |||
[[Category: Knight SD]] | |||
Latest revision as of 15:17, 24 January 2024
Crystal structure of an asymmetric dimer of the N-terminal domain of Euprosthenops australis Major Ampullate Spidroin 1 (dragline silk)Crystal structure of an asymmetric dimer of the N-terminal domain of Euprosthenops australis Major Ampullate Spidroin 1 (dragline silk)
Structural highlights
FunctionPublication Abstract from PubMedSpider silk is a biomaterial with exceptional mechanical toughness, and there is great interest in developing biomimetic methods to produce engineered spider silk-based materials. However, the mechanisms that regulate the conversion of spider silk proteins (spidroins) from highly soluble dope into silk are not completely understood. The N-terminal domain (NT) of Euprosthenops australis dragline silk protein undergoes conformational and quaternary-structure changes from a monomer at a pH above 7 to a homodimer at lower pH values. Conversion from the monomer to the dimer requires the protonation of three conserved glutamic acid residues, resulting in a low-pH `locked' dimer stabilized by symmetric electrostatic interactions at the poles of the dimer. The detailed molecular events during this transition are still unresolved. Here, a 2.1 A resolution crystal structure of an NT T61A mutant in an alternative, asymmetric, dimer form in which the electrostatic interactions at one of the poles are dramatically different from those in symmetrical dimers is presented. A similar asymmetric dimer structure from dragline silk of Nephila clavipes has previously been described. It is suggested that asymmetric dimers represent a conserved intermediate state in spider silk formation, and a revised `lock-and-trigger' mechanism for spider silk formation is presented. Structure of the N-terminal domain of Euprosthenops australis dragline silk suggests that conversion of spidroin dope to spider silk involves a conserved asymmetric dimer intermediate.,Jiang W, Askarieh G, Shkumatov A, Hedhammar M, Knight SD Acta Crystallogr D Struct Biol. 2019 Jul 1;75(Pt 7):618-627. doi:, 10.1107/S2059798319007253. Epub 2019 Jun 26. PMID:31282471[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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