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2wit

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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 Corynebacterium glutamicum. 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.
Method:	X-ray diffraction, Resolution 3.35Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 1: / Line 1: @@
 ==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=''>
+<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 [http://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WIT FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BET:TRIMETHYL+GLYCINE'>BET</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]] 3.35&#8491;</td></tr>
-<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='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='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'>[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>
-<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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wit ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BETP_CORGL BETP_CORGL]] High-affinity uptake of glycine betaine (By similarity).
+[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]]
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Micrococcus glutamicus kinoshita et al. 1958]]
+[[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]]

2wit

From Proteopedia

Current revision

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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