4xtt: Difference between revisions
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<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 == | ||
<table><tr><td colspan='2'>[[4xtt]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xtt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_08BA02176 Staphylococcus aureus 08BA02176]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XTT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2BA:(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-3,5,10,12-TETROL+5,12-DIOXIDE'>2BA</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.708Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2BA:(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-3,5,10,12-TETROL+5,12-DIOXIDE'>2BA</scene></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=4xtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xtt OCA], [https://pdbe.org/4xtt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xtt RCSB], [https://www.ebi.ac.uk/pdbsum/4xtt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xtt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0M3KL06_STAAU A0A0M3KL06_STAAU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Staphylococcus aureus | [[Category: Staphylococcus aureus 08BA02176]] | ||
[[Category: Choi | [[Category: Choi BS]] | ||
[[Category: Kim | [[Category: Kim H]] | ||
[[Category: Kim | [[Category: Kim SO]] | ||
[[Category: Ko | [[Category: Ko J]] | ||
[[Category: Lee | [[Category: Lee JO]] | ||
[[Category: Youn | [[Category: Youn SJ]] | ||
Latest revision as of 18:31, 8 November 2023
Structural Studies of Potassium Transport Protein KtrA Regulator of Conductance of K+ (RCK) C domain in Complex with Cyclic Diadenosine Monophosphate (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)
Structural highlights
FunctionPublication Abstract from PubMedAlthough 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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