4bpq: Difference between revisions
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<StructureSection load='4bpq' size='340' side='right'caption='[[4bpq]], [[Resolution|resolution]] 6.00Å' scene=''> | <StructureSection load='4bpq' size='340' side='right'caption='[[4bpq]], [[Resolution|resolution]] 6.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bpq]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4bpq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BPQ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 6Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bpq OCA], [https://pdbe.org/4bpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bpq RCSB], [https://www.ebi.ac.uk/pdbsum/4bpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bpq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Symporter|Symporter]] | *[[Symporter 3D structures|Symporter 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Klebsiella pneumoniae]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arheit | [[Category: Arheit M]] | ||
[[Category: Gruetter | [[Category: Gruetter MG]] | ||
[[Category: Kebbel | [[Category: Kebbel F]] | ||
[[Category: Kurz | [[Category: Kurz M]] | ||
[[Category: Stahlberg | [[Category: Stahlberg H]] | ||
Latest revision as of 14:03, 9 May 2024
Structure and substrate induced conformational changes of the secondary citrate-sodium symporter CitS revealed by electron crystallographyStructure and substrate induced conformational changes of the secondary citrate-sodium symporter CitS revealed by electron crystallography
Structural highlights
Publication Abstract from PubMedThe secondary Na+/citrate symporter CitS of Klebsiella pneumoniae is the best-characterized member of the 2-hydroxycarboxylate transporter family. The recent projection structure gave insight into its overall structural organization. Here, we present the three-dimensional map of dimeric CitS obtained with electron crystallography. Each monomer has 13 alpha-helical transmembrane segments; six are organized in a distal helix cluster and seven in the central dimer interface domain. Based on structural analyses and comparison to VcINDY, we propose a molecular model for CitS, assign the helices, and demonstrate the internal structural symmetry. We also present projections of CitS in several conformational states induced by the presence and absence of sodium and citrate as substrates. Citrate binding induces a defined movement of alpha helices within the distal helical cluster. Based on this, we propose a substrate translocation site and conformational changes that are in agreement with the transport model of "alternating access". Structure and Substrate-Induced Conformational Changes of the Secondary Citrate/Sodium Symporter CitS Revealed by Electron Crystallography.,Kebbel F, Kurz M, Arheit M, Grutter MG, Stahlberg H Structure. 2013 Jun 25. pii: S0969-2126(13)00193-7. doi:, 10.1016/j.str.2013.05.011. PMID:23810698[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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