2wit

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Revision as of 02:06, 10 February 2016

CRYSTAL STRUCTURE OF THE SODIUM-COUPLED GLYCINE BETAINE SYMPORTER BETP FROM CORYNEBACTERIUM GLUTAMICUM WITH BOUND SUBSTRATE

Structural highlights

2wit is a 3 chain structure with sequence from "micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958. This structure supersedes the now removed PDB entry 2w8a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2w8a
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[BETP_CORGL] High-affinity uptake of glycine betaine (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ressl S, Terwisscha van Scheltinga AC, Vonrhein C, Ott V, Ziegler C. Molecular basis of transport and regulation in the Na(+)/betaine symporter BetP. Nature. 2009 Mar 5;458(7234):47-52. PMID:19262666 doi:10.1038/nature07819

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wit"

@@ Line 6: / Line 6: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2w8a|2w8a]]</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=2wit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wit OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wit RCSB], [http://www.ebi.ac.uk/pdbsum/2wit PDBsum]</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=2wit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wit OCA], [http://pdbe.org/2wit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wit RCSB], [http://www.ebi.ac.uk/pdbsum/2wit PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 18: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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;">
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2wit" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2wit

From Proteopedia

Revision as of 02:06, 10 February 2016

CRYSTAL STRUCTURE OF THE SODIUM-COUPLED GLYCINE BETAINE SYMPORTER BETP FROM CORYNEBACTERIUM GLUTAMICUM WITH BOUND SUBSTRATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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