Structural highlights
Publication Abstract from PubMed
Alba (Acetylation lowers binding affinity) domain is a small, dimeric nucleic acid-binding domain, which is widely distributed in archaea and numbers of eukaryotes. Alba domain containing proteins have been reported to be involved in many cellular processes, such as regulation of translation, maintaining genome stability, regulation of RNA processing and so on. In Trypanosoma brucei (T. brucei), there are four Alba proteins identified, which are named TbAlba1 to TbAlba4. However, the structure and function of TbAlba proteins are still unknown. Here, we solved the crystal structure of TbAlba1 to a resolution of 2.46 A. TbAlba1 adopts a similar Alba-fold, which comprises of four beta-strands (beta1-beta4) and three long alpha-helices (alpha1-alpha3). Furthermore, TbAlba1 displays some structural features quite different from other Alba proteins. These differences may imply the diverse biological roles of Alba family members.
Crystal structure of TbAlba1 from Trypanosoma brucei.,Gao J, Xiao C, Liao S, Tu X J Struct Biol. 2021 Jun 6;213(3):107751. doi: 10.1016/j.jsb.2021.107751. PMID:34107324[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gao J, Xiao C, Liao S, Tu X. Crystal structure of TbAlba1 from Trypanosoma brucei. J Struct Biol. 2021 Jun 6;213(3):107751. doi: 10.1016/j.jsb.2021.107751. PMID:34107324 doi:http://dx.doi.org/10.1016/j.jsb.2021.107751
