Structural highlights
Function
[ALBA2_AERPE] Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity).
Publication Abstract from PubMed
DNA binding proteins are essential in all organisms, and they play important roles in both compacting and regulating the genetic material. All thermophilic and hyperthermophilic archaea encode one or more copies of Alba or Sso10b, which is a small, abundant, basic protein that binds DNA. Here, we present the crystal structure of Ape10b2 from Aeropyrum pernix K1 at 1.70 A. Although the overall structure resembles the known Alba protein fold, a significant conformational change was observed in the loop regions. Specifically, the L5 loop is slightly longer, as compared to those of other known proteins, and the flexibility of this loop may facilitate the interaction with double stranded DNA. In addition, we showed that Ape10b2 binds to 16 and 39 bp duplex DNAs with high affinity. On the basis of our analyses, we have created a putative protein-DNA complex model.
Crystal structure of an archaeal specific DNA-binding protein (Ape10b2) from Aeropyrum pernix K1.,Kumarevel T, Sakamoto K, Gopinath SC, Shinkai A, Kumar PK, Yokoyama S Proteins. 2008 May 15;71(3):1156-62. PMID:18004791[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kumarevel T, Sakamoto K, Gopinath SC, Shinkai A, Kumar PK, Yokoyama S. Crystal structure of an archaeal specific DNA-binding protein (Ape10b2) from Aeropyrum pernix K1. Proteins. 2008 May 15;71(3):1156-62. PMID:18004791 doi:10.1002/prot.21807
