6Q2Z

NMR solution structure of the HVO_2922 protein from Haloferax volcanii

6Q2Z の概要

• エントリーDOI: 10.2210/pdb6q2z/pdb
• NMR情報: BMRB: 34334
• 分子名称: UPF0339 family protein (1 entity in total)
• 機能のキーワード: conserved hypothetical protein, unknown function
• 由来する生物種: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13372.83

構造登録者

Kubatova, N.,Jonker, H.R.A.,Saxena, K.,Richter, C.,Marchfelder, A.,Schwalbe, H. (登録日: 2018-12-03, 公開日: 2019-06-12, 最終更新日: 2024-07-03)

主引用文献

Kubatova, N.,Jonker, H.R.A.,Saxena, K.,Richter, C.,Vogel, V.,Schreiber, S.,Marchfelder, A.,Schwalbe, H.
Solution Structure and Dynamics of the Small Protein HVO_2922 from Haloferax volcanii.
Chembiochem, 21:149-156, 2020

PubMed Abstract: Past sequencing campaigns overlooked small proteins as they seemed to be irrelevant due to their small size. However, their occurrence is widespread, and there is growing evidence that these small proteins are in fact functionally very important in organisms found in all kingdoms of life. Within a global proteome analysis for small proteins of the archaeal model organism Haloferax volcanii, the HVO_2922 protein has been identified. It is differentially expressed in response to changes in iron and salt concentrations, thus suggesting that its expression is stress-regulated. The protein is conserved among Haloarchaea and contains an uncharacterized domain of unknown function (DUF1508, UPF0339 family protein). We elucidated the NMR solution structure, which shows that the isolated protein forms a symmetrical dimer. The dimerization is found to be concentration-dependent and essential for protein stability and most likely for its functionality, as mutagenesis at the dimer interface leads to a decrease in stability and protein aggregation.

PubMed: 31161645
DOI: 10.1002/cbic.201900085

実験手法

SOLUTION NMR