1bg5: Difference between revisions

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-{{Seed}}
-[[Image:1bg5.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE==
-The line below this paragraph, containing "STRUCTURE_1bg5", creates the "Structure Box" on the page.
+<StructureSection load='1bg5' size='340' side='right'caption='[[1bg5]], [[Resolution|resolution]] 2.60&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'>[[1bg5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BG5 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]] 2.6&#8491;</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=1bg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg5 OCA], [https://pdbe.org/1bg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bg5 RCSB], [https://www.ebi.ac.uk/pdbsum/1bg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bg5 ProSAT]</span></td></tr>
-{{STRUCTURE_1bg5|  PDB=1bg5  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.  GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
+== 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/bg/1bg5_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=1bg5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The ankyrin 33-residue repeating motif, an L-shaped structure with protruding beta-hairpin tips, mediates specific macromolecular interactions with cytoskeletal, membrane, and regulatory proteins. The association between ankyrin and alpha-Na,K-ATPase, a ubiquitous membrane protein critical to vectorial transport of ions and nutrients, is required to assemble and stabilize Na,K-ATPase at the plasma membrane. alpha-Na,K-ATPase binds both red cell ankyrin (AnkR, a product of the ANK1 gene) and Madin-Darby canine kidney cell ankyrin (AnkG, a product of the ANK3 gene) utilizing residues 142-166 (SYYQEAKSSKIMESFK NMVPQQALV) in its second cytoplasmic domain. Fusion peptides of glutathione S-transferase incorporating these 25 amino acids bind specifically to purified ankyrin (Kd = 118 +/- 50 nM). The three-dimensional structure (2.6 A) of this minimal ankyrin-binding motif, crystallized as the fusion protein, reveals a 7-residue loop with one charged hydrophilic face capping a double beta-strand. Comparison with ankyrin-binding sequences in p53, CD44, neurofascin/L1, and the inositol 1,4,5-trisphosphate receptor suggests that the valency and specificity of ankyrin binding is achieved by the interaction of 5-7-residue surface loops with the beta-hairpin tips of multiple ankyrin repeat units.
-===CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE===
+Structure of the ankyrin-binding domain of alpha-Na,K-ATPase.,Zhang Z, Devarajan P, Dorfman AL, Morrow JS J Biol Chem. 1998 Jul 24;273(30):18681-4. PMID:9668035<ref>PMID:9668035</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_9668035}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1bg5" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 9668035 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9668035}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-BG5 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG5 OCA].
-==Reference==
-<ref group="xtra">PMID:9668035</ref><references group="xtra"/>
 [[Category: Rattus norvegicus]]
-[[Category: Devarajan, P.]]
+[[Category: Devarajan P]]
-[[Category: Morrow, J S.]]
+[[Category: Morrow JS]]
-[[Category: Zhang, Z.]]
+[[Category: Zhang Z]]
-[[Category: Ankyrin binding]]
-[[Category: Atpase]]
-[[Category: Carrier crystallization]]
-[[Category: Glutathione-s-transferase]]
-[[Category: Ion transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:49:54 2009''