2wpq: Difference between revisions

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-[[Image:2wpq.png|left|200px]]
-<!--
+==Salmonella enterica SadA 479-519 fused to GCN4 adaptors (SadAK3, in- register fusion)==
-The line below this paragraph, containing "STRUCTURE_2wpq", creates the "Structure Box" on the page.
+<StructureSection load='2wpq' size='340' side='right'caption='[[2wpq]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2wpq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WPQ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
-{{STRUCTURE_2wpq|  PDB=2wpq  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wpq OCA], [https://pdbe.org/2wpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wpq RCSB], [https://www.ebi.ac.uk/pdbsum/2wpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wpq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SADA_SALTY SADA_SALTY] Involved in cell aggregation, biofilm formation, and adhesion to human intestinal epithelial cells.<ref>PMID:21859856</ref>
+== 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/wp/2wpq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2wpq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Most core residues of coiled coils are hydrophobic. Occasional polar residues are thought to lower stability, but impart structural specificity. The coiled coils of trimeric autotransporter adhesins (TAAs) are conspicuous for their large number of polar residues in position d of the core, which often leads to their prediction as natively unstructured regions. The most frequent residue, asparagine (N@d), can occur in runs of up to 19 consecutive heptads, frequently in the motif [I/V]xxNTxx. In the Salmonella TAA, SadA, the core asparagines form rings of interacting residues with the following threonines, grouped around a central anion. This conformation is observed generally in N@d layers from trimeric coiled coils of known structure. Attempts to impose a different register on the motif show that the asparagines orient themselves specifically into the core, even against conflicting information from flanking domains. When engineered into the GCN4 leucine zipper, N@d layers progressively destabilized the structure, but zippers with 3 N@d layers still folded at high concentration. We propose that N@d layers maintain the coiled coils of TAAs in a soluble, export-competent state during autotransport through the outer membrane. More generally, we think that polar motifs that are both periodic and conserved may often reflect special folding requirements, rather than an unstructured state of the mature proteins.
-===SALMONELLA ENTERICA SADA 479-519 FUSED TO GCN4 ADAPTORS (SADAK3, IN-REGISTER FUSION)===
+A coiled-coil motif that sequesters ions to the hydrophobic core.,Hartmann MD, Ridderbusch O, Zeth K, Albrecht R, Testa O, Woolfson DN, Sauer G, Dunin-Horkawicz S, Lupas AN, Alvarez BH Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):16950-5. Epub 2009 Sep 23. PMID:19805097<ref>PMID:19805097</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2wpq" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19805097}}, adds the Publication Abstract to the page
+*[[Adhesin 3D structures|Adhesin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19805097 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19805097}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[2wpq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WPQ OCA].
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
+[[Category: Albrecht R]]
-==Reference==
+[[Category: Hartmann MD]]
-<ref group="xtra">PMID:19805097</ref><ref group="xtra">PMID:18093992</ref><references group="xtra"/>
+[[Category: Hernandez Alvarez B]]
-[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
+[[Category: Lupas AN]]
-[[Category: Albrecht, R.]]
+[[Category: Zeth K]]
-[[Category: Alvarez, B Hernandez.]]
-[[Category: Hartmann, M D.]]
-[[Category: Lupas, A N.]]
-[[Category: Zeth, K.]]
-[[Category: Coiled coil]]
-[[Category: Hydrophobic core]]
-[[Category: Ion coordination]]
-[[Category: Membrane protein]]
-[[Category: Polar core residue]]
-[[Category: Protein export]]
-[[Category: Taa]]
-[[Category: Trimeric autotransporter adhesin]]