2wit: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2wit.png|left|200px]]
-{{STRUCTURE_2wit|  PDB=2wit  |  SCENE=  }}
+==CRYSTAL STRUCTURE OF THE SODIUM-COUPLED GLYCINE BETAINE SYMPORTER BETP FROM CORYNEBACTERIUM GLUTAMICUM WITH BOUND SUBSTRATE==
+<StructureSection load='2wit' size='340' side='right'caption='[[2wit]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2wit]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2w8a 2w8a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WIT 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]] 3.35&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BET:TRIMETHYL+GLYCINE'>BET</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2wit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wit OCA], [https://pdbe.org/2wit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wit RCSB], [https://www.ebi.ac.uk/pdbsum/2wit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wit ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BETP_CORGL BETP_CORGL] High-affinity uptake of glycine betaine (By similarity).
+== 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/wi/2wit_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=2wit ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Osmoregulated transporters sense intracellular osmotic pressure and respond to hyperosmotic stress by accumulation of osmolytes to restore normal hydration levels. Here we report the determination of the X-ray structure of a member of the family of betaine/choline/carnitine transporters, the Na(+)-coupled symporter BetP from Corynebacterium glutamicum, which is a highly effective osmoregulated uptake system for glycine betaine. Glycine betaine is bound in a tryptophan box occluded from both sides of the membrane with aromatic side chains lining the transport pathway. BetP has the same overall fold as three unrelated Na(+)-coupled symporters. Whereas these are crystallized in either the outward-facing or the inward-facing conformation, the BetP structure reveals a unique intermediate conformation in the Na(+)-coupled transport cycle. The trimeric architecture of BetP and the break in three-fold symmetry by the osmosensing C-terminal helices suggest a regulatory mechanism of Na(+)-coupled osmolyte transport to counteract osmotic stress.
-===CRYSTAL STRUCTURE OF THE SODIUM-COUPLED GLYCINE BETAINE SYMPORTER BETP FROM CORYNEBACTERIUM GLUTAMICUM WITH BOUND SUBSTRATE===
+Molecular basis of transport and regulation in the Na(+)/betaine symporter BetP.,Ressl S, Terwisscha van Scheltinga AC, Vonrhein C, Ott V, Ziegler C Nature. 2009 Mar 5;458(7234):47-52. PMID:19262666<ref>PMID:19262666</ref>
-{{ABSTRACT_PUBMED_23318153}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2wit" style="background-color:#fffaf0;"></div>
-[[2wit]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2w8a 2w8a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WIT OCA].
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:019262666</ref><references group="xtra"/>
+</StructureSection>
 [[Category: Corynebacterium glutamicum]]
-[[Category: Ott, V.]]
+[[Category: Large Structures]]
-[[Category: Ressl, S.]]
+[[Category: Ott V]]
-[[Category: Scheltinga, A C.Terwisscha Van.]]
+[[Category: Ressl S]]
-[[Category: Vonrhein, C.]]
+[[Category: Terwisscha Van Scheltinga AC]]
-[[Category: Ziegler, C.]]
+[[Category: Vonrhein C]]
-[[Category: Betaine transport]]
+[[Category: Ziegler C]]
-[[Category: Cell membrane]]
-[[Category: Chemosensor and osmosensor]]
-[[Category: Hyperosmotic stress]]
-[[Category: Membrane]]
-[[Category: Membrane protein]]
-[[Category: Secondary transporter]]
-[[Category: Sodium coupled transport]]
-[[Category: Transmembrane]]
-[[Category: Transport]]
-[[Category: Trimer]]