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4j9u

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Revision as of 10:14, 25 December 2014

Crystal Structure of the TrkH/TrkA potassium transport complex

Structural highlights

4j9u is a 8 chain structure with sequence from Vibrio parahaemolyticus rimd 2210633. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4j9v
Gene:	trkH, VP0032 (Vibrio parahaemolyticus RIMD 2210633), VP3045 (Vibrio parahaemolyticus RIMD 2210633)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[TRKH_VIBPA] Low-affinity potassium transport system. Interacts with trk system potassium uptake protein TrkA and requires TrkE for transport activity. Selective for permeation of potassium ion and rubidium ion over smaller ions such as natrium or litium.

Publication Abstract from PubMed

TrkH belongs to a superfamily of K(+) transport proteins required for growth of bacteria in low external K(+) concentrations. The crystal structure of TrkH from Vibrio parahaemolyticus showed that TrkH resembles a K(+) channel and may have a gating mechanism substantially different from K(+) channels. TrkH assembles with TrkA, a cytosolic protein comprising two RCK (regulate the conductance of K(+)) domains, which are found in certain K(+) channels and control their gating. However, fundamental questions on whether TrkH is an ion channel and how it is regulated by TrkA remain unresolved. Here we show single-channel activity of TrkH that is upregulated by ATP via TrkA. We report two structures of the tetrameric TrkA ring, one in complex with TrkH and one in isolation, in which the ring assumes two markedly different conformations. These results suggest a mechanism for how ATP increases TrkH activity by inducing conformational changes in TrkA.

Gating of the TrkH ion channel by its associated RCK protein TrkA.,Cao Y, Pan Y, Huang H, Jin X, Levin EJ, Kloss B, Zhou M Nature. 2013 Apr 18;496(7445):317-22. doi: 10.1038/nature12056. PMID:23598339^[1]

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

References

↑ Cao Y, Pan Y, Huang H, Jin X, Levin EJ, Kloss B, Zhou M. Gating of the TrkH ion channel by its associated RCK protein TrkA. Nature. 2013 Apr 18;496(7445):317-22. doi: 10.1038/nature12056. PMID:23598339 doi:http://dx.doi.org/10.1038/nature12056

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4j9u"

@@ Line 8: / Line 8: @@
 <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=4j9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j9u RCSB], [http://www.ebi.ac.uk/pdbsum/4j9u PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TRKH_VIBPA TRKH_VIBPA]] Low-affinity potassium transport system. Interacts with trk system potassium uptake protein TrkA and requires TrkE for transport activity. Selective for permeation of potassium ion and rubidium ion over smaller ions such as natrium or litium.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4j9u

From Proteopedia

Revision as of 10:14, 25 December 2014

Crystal Structure of the TrkH/TrkA potassium transport complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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