3lr8: Difference between revisions

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OCA

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 ==Self-assembly of spider silk proteins is controlled by a pH-sensitive relay==
-<StructureSection load='3lr8' size='340' side='right' caption='[[3lr8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='3lr8' size='340' side='right'caption='[[3lr8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3lr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Euprosthenops_australis Euprosthenops australis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LR8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3lr8]] is a 2 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=3LR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LR8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lr2|3lr2]], [[3lr6|3lr6]], [[3lrd|3lrd]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MaSp1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=332052 Euprosthenops australis])</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=3lr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lr8 OCA], [https://pdbe.org/3lr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lr8 RCSB], [https://www.ebi.ac.uk/pdbsum/3lr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lr8 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lr8 OCA], [http://pdbe.org/3lr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lr8 RCSB], [http://www.ebi.ac.uk/pdbsum/3lr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lr8 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q05H60_9ARAC Q05H60_9ARAC]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lr/3lr8_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lr/3lr8_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 19: / Line 20: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lr8 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Nature's high-performance polymer, spider silk, consists of specific proteins, spidroins, with repetitive segments flanked by conserved non-repetitive domains. Spidroins are stored as a highly concentrated fluid dope. On silk formation, intermolecular interactions between repeat regions are established that provide strength and elasticity. How spiders manage to avoid premature spidroin aggregation before self-assembly is not yet established. A pH drop to 6.3 along the spider's spinning apparatus, altered salt composition and shear forces are believed to trigger the conversion to solid silk, but no molecular details are known. Miniature spidroins consisting of a few repetitive spidroin segments capped by the carboxy-terminal domain form metre-long silk-like fibres irrespective of pH. We discovered that incorporation of the amino-terminal domain of major ampullate spidroin 1 from the dragline of the nursery web spider Euprosthenops australis (NT) into mini-spidroins enables immediate, charge-dependent self-assembly at pH values around 6.3, but delays aggregation above pH 7. The X-ray structure of NT, determined to 1.7 A resolution, shows a homodimer of dipolar, antiparallel five-helix bundle subunits that lack homologues. The overall dimeric structure and observed charge distribution of NT is expected to be conserved through spider evolution and in all types of spidroins. Our results indicate a relay-like mechanism through which the N-terminal domain regulates spidroin assembly by inhibiting precocious aggregation during storage, and accelerating and directing self-assembly as the pH is lowered along the spider's silk extrusion duct.
-Self-assembly of spider silk proteins is controlled by a pH-sensitive relay.,Askarieh G, Hedhammar M, Nordling K, Saenz A, Casals C, Rising A, Johansson J, Knight SD Nature. 2010 May 13;465(7295):236-8. PMID:20463740<ref>PMID:20463740</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3lr8" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Euprosthenops australis]]
-[[Category: Askarieh, G]]
+[[Category: Large Structures]]
-[[Category: Hedhammar, H]]
+[[Category: Askarieh G]]
-[[Category: Johansson, J]]
+[[Category: Hedhammar H]]
-[[Category: Knight, S D]]
+[[Category: Johansson J]]
-[[Category: Nordling, K]]
+[[Category: Knight SD]]
-[[Category: Rising, A]]
+[[Category: Nordling K]]
-[[Category: Dragline spider silk]]
+[[Category: Rising A]]
-[[Category: Nt e79q mutant]]
-[[Category: Ph-dependence]]
-[[Category: Self-assembly]]
-[[Category: Structural protein]]