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| | ==Structure of RCK domain with cda== | | ==Structure of RCK domain with cda== |
| - | <StructureSection load='5f29' size='340' side='right' caption='[[5f29]], [[Resolution|resolution]] 1.82Å' scene=''> | + | <StructureSection load='5f29' size='340' side='right'caption='[[5f29]], [[Resolution|resolution]] 1.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5f29]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F29 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5f29]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F29 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.821Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ys2|4ys2]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5f29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f29 OCA], [https://pdbe.org/5f29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f29 RCSB], [https://www.ebi.ac.uk/pdbsum/5f29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f29 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kefC, ERS154949_00406 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=5f29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f29 OCA], [http://pdbe.org/5f29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f29 RCSB], [http://www.ebi.ac.uk/pdbsum/5f29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f29 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2FZQ4_STAA8 Q2FZQ4_STAA8] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chin, K H]] | + | [[Category: Large Structures]] |
| - | [[Category: Cda]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Cpaa]] | + | [[Category: Chin KH]] |
| - | [[Category: Rck domain]]
| + | |
| - | [[Category: Transport protein]]
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| Structural highlights
Function
Q2FZQ4_STAA8
Publication Abstract from PubMed
Cyclic di-AMP (c-di-AMP) is a relatively new member of the family of bacterial cyclic dinucleotide second messengers. It has attracted significant attention in recent years because of the abundant roles it plays in a variety of Gram-positive bacteria. The structural features that allow diverse bacterial proteins to bind c-di-AMP are not fully understood. Here we report the biophysical and structural studies of c-di-AMP in complex with a bacterial cation-proton antiporter (CpaA) RCK (regulator of the conductance of K(+)) protein from Staphylococcus aureus (Sa). The crystal structure of the SaCpaA_RCK C-terminal domain (CTD) in complex with c-di-AMP was determined to a resolution of 1.81 A. This structure revealed two well-liganded water molecules, each interacting with one of the adenine bases by a unique H2Olp-pi interaction to stabilize the complex. Sequence blasting using the SaCpaA_RCK primary sequence against the bacterial genome database returned many CpaA analogues, and alignment of these sequences revealed that the active site residues are all well-conserved, indicating a universal c-di-AMP binding mode for CpaA_RCK. A proteoliposome activity assay using the full-length SaCpaA membrane protein indicated that c-di-AMP binding alters its antiporter activity by approximately 40%. A comparison of this structure to all other reported c-di-AMP-receptor complex structures revealed that c-di-AMP binds to receptors in either a "U-shape" or "V-shape" mode. The two adenine rings are stabilized in the inner interaction zone by a variety of CH-pi, cation-pi, backbone-pi, or H2Olp-pi interaction, but more commonly in the outer interaction zone by hydrophobic CH-pi or pi-pi interaction. The structures determined to date provide an understanding of the mechanisms by which a single c-di-AMP can interact with a variety of receptor proteins, and how c-di-AMP binds receptor proteins in a special way different from that of c-di-GMP.
Structural Insights into the Distinct Binding Mode of Cyclic Di-AMP with SaCpaA_RCK.,Chin KH, Liang JM, Yang JG, Shih MS, Tu ZL, Wang YC, Sun XH, Hu NJ, Liang ZX, Dow JM, Ryan RP, Chou SH Biochemistry. 2015 Aug 11;54(31):4936-51. doi: 10.1021/acs.biochem.5b00633. Epub , 2015 Jul 27. PMID:26171638[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chin KH, Liang JM, Yang JG, Shih MS, Tu ZL, Wang YC, Sun XH, Hu NJ, Liang ZX, Dow JM, Ryan RP, Chou SH. Structural Insights into the Distinct Binding Mode of Cyclic Di-AMP with SaCpaA_RCK. Biochemistry. 2015 Aug 11;54(31):4936-51. doi: 10.1021/acs.biochem.5b00633. Epub , 2015 Jul 27. PMID:26171638 doi:http://dx.doi.org/10.1021/acs.biochem.5b00633
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