4xtt
From Proteopedia
(Difference between revisions)
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| - | ==Structural Studies of Potassium Transport Protein KtrA in Complex with c-di-AMP== | + | ==Structural Studies of Potassium Transport Protein KtrA Regulator of Conductance of K+ (RCK) C domain in Complex with Cyclic Diadenosine Monophosphate (c-di-AMP)== |
<StructureSection load='4xtt' size='340' side='right' caption='[[4xtt]], [[Resolution|resolution]] 2.71Å' scene=''> | <StructureSection load='4xtt' size='340' side='right' caption='[[4xtt]], [[Resolution|resolution]] 2.71Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<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=4xtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xtt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xtt RCSB], [http://www.ebi.ac.uk/pdbsum/4xtt 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=4xtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xtt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xtt RCSB], [http://www.ebi.ac.uk/pdbsum/4xtt PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Although it was only recently identified as a second messenger, c-di-AMP was found to have fundamental importance in numerous bacterial functions such as ion transport. The potassium transporter protein, KtrA, was identified as a c-di-AMP receptor. However, the cocrystallization of c-di-AMP with the protein has not been studied. Here, we determined the crystal structure of KtrA RCK_C domain in complex with c-di-AMP. The c-di-AMP nucleotide, which adopts a U-shaped conformation, is bound at the dimer interface of RCK_ C close to helices alpha3 and alpha4. c-di-AMP interacts with KtrA RCK_C mainly by forming hydrogen bonds and hydrophobic interactions. c-di-AMP binding induces the contraction of the dimer, bringing the two monomers of KtrA RCK_C into close proximity. The KtrA RCK_C was able to interact with only c-di-AMP, but not with c-di-GMP, 3'3-cGAMP, ATP and ADP. The structure of KtrA RCK_C domain and c-di-AMP complex would expand our understanding about the mechanism of inactivation in Ktr transporters governed by c-di-AMP. | ||
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| + | Structural Studies of Potassium Transport Protein KtrA Regulator of Conductance of K+ (RCK) C domain in Complex with Cyclic Diadenosine Monophosphate (c-di-AMP).,Kim H, Youn SJ, Kim SO, Ko J, Lee JO, Choi BS J Biol Chem. 2015 May 7. pii: jbc.M115.641340. PMID:25957408<ref>PMID:25957408</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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[[Category: Ktra]] | [[Category: Ktra]] | ||
[[Category: Potassium]] | [[Category: Potassium]] | ||
| + | [[Category: Transport protein]] | ||
[[Category: Transporter]] | [[Category: Transporter]] | ||
Revision as of 10:12, 27 May 2015
Structural Studies of Potassium Transport Protein KtrA Regulator of Conductance of K+ (RCK) C domain in Complex with Cyclic Diadenosine Monophosphate (c-di-AMP)
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Categories: Choi, B S | Kim, H | Kim, S O | Ko, J | Lee, J O | Youn, S J | C-di-amp | Ktra | Potassium | Transport protein | Transporter
