7DL8

Crystal structure of ALBA1 from Trypanosoma brucei

Summary for 7DL8

• Entry DOI: 10.2210/pdb7dl8/pdb
• Descriptor: ALBA-Domain Protein (2 entities in total)
• Functional Keywords: alba domain, rna binding, rna binding protein
• Biological source: Trypanosoma brucei
• Total number of polymer chains: 4
• Total formula weight: 61061.25

Authors

Liao, S.,Gao, J.,Tu, X. (deposition date: 2020-11-26, release date: 2021-06-23, Last modification date: 2024-04-03)

Primary citation

Gao, J.,Xiao, C.,Liao, S.,Tu, X.
Crystal structure of TbAlba1 from Trypanosoma brucei.
J.Struct.Biol., 213:107751-107751, 2021

PubMed Abstract: 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 Å. TbAlba1 adopts a similar Alba-fold, which comprises of four β-strands (β1-β4) and three long α-helices (α1-α3). Furthermore, TbAlba1 displays some structural features quite different from other Alba proteins. These differences may imply the diverse biological roles of Alba family members.

PubMed: 34107324
DOI: 10.1016/j.jsb.2021.107751

Experimental method

X-RAY DIFFRACTION (2.459 Å)