5a1s

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5a1s is ON HOLD
+
==Crystal structure of the sodium-dependent citrate symporter SeCitS form Salmonella enterica.==
 +
<StructureSection load='5a1s' size='340' side='right' caption='[[5a1s]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5a1s]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1S FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene>, <scene name='pdbligand=UND:UNDECANE'>UND</scene></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=5a1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1s OCA], [http://pdbe.org/5a1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a1s RCSB], [http://www.ebi.ac.uk/pdbsum/5a1s PDBsum]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/G4BX92_SALIN G4BX92_SALIN]] Uptake of citrate across the boundary membrane with the concomitant uptake of a sodium ion (symport system).[PIRNR:PIRNR005348]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The common human pathogen Salmonella enterica takes up citrate as a nutrient via the sodium symporter SeCitS. Uniquely, our 2.5 A x-ray structure of the SeCitS dimer shows three different conformations of the active protomer. One protomer is in the outside-facing state. Two are in different inside-facing states. All three states resolve the substrates in their respective binding environments. Together with comprehensive functional studies on reconstituted proteoliposomes, the structures explain the transport mechanism in detail. Our results indicate a six-step process, with a rigid-body 31 degrees rotation of a helix bundle that translocates the bound substrates by 16 A across the membrane. Similar transport mechanisms may apply to a wide variety of related and unrelated secondary transporters, including important drug targets.
-
Authors: Woehlert, D., Groetzinger, M.J., Kuhlbrandt, W., Yildiz, O.
+
Mechanism of Na(+)-dependent citrate transport from the structure of an asymmetrical CitS dimer.,Wohlert D, Grotzinger MJ, Kuhlbrandt W, Yildiz O Elife. 2015 Dec 4;4. pii: e09375. doi: 10.7554/eLife.09375. PMID:26636752<ref>PMID:26636752</ref>
-
Description: Crystal structure of the sodium-dependent citrate symporter SeCitS form Salmonella enterica.
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Yildiz, O]]
+
<div class="pdbe-citations 5a1s" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Groetzinger, M J]]
[[Category: Kuhlbrandt, W]]
[[Category: Kuhlbrandt, W]]
[[Category: Woehlert, D]]
[[Category: Woehlert, D]]
-
[[Category: Groetzinger, M.J]]
+
[[Category: Yildiz, O]]
 +
[[Category: Di-carboxylate transporter]]
 +
[[Category: Membrane protein]]
 +
[[Category: Symporter]]
 +
[[Category: Transport protein]]
 +
[[Category: Transporter]]

Revision as of 02:40, 21 February 2016

Crystal structure of the sodium-dependent citrate symporter SeCitS form Salmonella enterica.

5a1s, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools