|
|
| Line 10: |
Line 10: |
| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q9F377_STRCO Q9F377_STRCO] | | [https://www.uniprot.org/uniprot/Q9F377_STRCO Q9F377_STRCO] |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| The important and diverse regulatory roles of Ca(2+) in eukaryotes are conveyed by the EF-hand containing calmodulin superfamily. However, the calcium-regulatory proteins in prokaryotes are still poorly understood. In this study, we report the three-dimensional structure of the calcium-binding protein from Streptomyces coelicolor, named CabD, which shares low sequence homology with other known helix-loop-helix EF-hand proteins. The CabD structure should provide insights into the biological role of the prokaryotic calcium-binding proteins. The unusual structural features of CabD compared with prokaryotic EF-hand proteins and eukaryotic sarcoplasmic calcium-binding proteins, including the bending conformation of the first C-terminal alpha-helix, unpaired ligand-binding EF-hands and the lack of the extreme C-terminal loop region, suggest it may have a distinct and significant function in calcium-mediated bacterial physiological processes, and provide a structural basis for potential calcium-mediated regulatory roles in prokaryotes.
| |
|
| |
| Structural basis for prokaryotic calcium-mediated regulation by a Streptomyces coelicolor calcium binding protein.,Zhao X, Pang H, Wang S, Zhou W, Yang K, Bartlam M Protein Cell. 2010 Aug;1(8):771-9. Epub 2010 Aug 28. PMID:21203918<ref>PMID:21203918</ref>
| |
|
| |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 3akb" style="background-color:#fffaf0;"></div>
| |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
