4wk3

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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=4wk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wk3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wk3 RCSB], [http://www.ebi.ac.uk/pdbsum/4wk3 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=4wk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wk3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wk3 RCSB], [http://www.ebi.ac.uk/pdbsum/4wk3 PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyclic-di-AMP (c-di-AMP) is a bacterial secondary messenger involved in various processes, including sensing of DNA-integrity, cell wall metabolism and potassium transport. A number of c-di-AMP receptor proteins have recently been identified in Staphylococcus aureus. One of them - PstA - possesses a ferredoxin-like fold and is structurally related to the class of PII signal-transduction proteins. PII proteins are involved in a large number of pathways, most of them associated with nitrogen metabolism. In this study we describe the mode of c-di-AMP binding and subsequent structural changes of S. aureus PstA. An altered architecture in PstA compared to canonical PII proteins results in differences in ligand coordination.
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c-di-AMP recognition by Staphylococcus aureus PstA.,Muller M, Hopfner KP, Witte G FEBS Lett. 2015 Jan 2;589(1):45-51. doi: 10.1016/j.febslet.2014.11.022. Epub 2014, Nov 28. PMID:25435171<ref>PMID:25435171</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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Revision as of 10:55, 24 December 2014

Structure of Staphyloccus aureus PstA

4wk3, resolution 2.60Å

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