2L52

Solution structure of the small archaeal modifier protein 1 (SAMP1) from Methanosarcina acetivorans

2L52 の概要

• エントリーDOI: 10.2210/pdb2l52/pdb
• NMR情報: BMRB: 17263
• 分子名称: METHANOSARCINA ACETIVORANS SAMP1 HOMOLOG (1 entity in total)
• 機能のキーワード: beta-grasp fold, protein binding, samp1, samp, e1-like, samp-activator, elsa, adenylation, ubiquitin
• 由来する生物種: Methanosarcina acetivorans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10708.40

構造登録者

Damberger, F.F.,Ranjan, N.,Sutter, M.,Allain, F.H.-T.,Weber-Ban, E. (登録日: 2010-10-24, 公開日: 2011-02-09, 最終更新日: 2024-05-15)

主引用文献

Ranjan, N.,Damberger, F.F.,Sutter, M.,Allain, F.H.,Weber-Ban, E.
Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins.
J.Mol.Biol., 405:1040-1055, 2011

PubMed Abstract: In archaea, two ubiquitin-like small archaeal modifier protein (SAMPs) were recently shown to be conjugated to proteins in vivo. SAMPs display homology to bacterial MoaD sulfur transfer proteins and eukaryotic ubiquitin-like proteins, and they share with them the conserved C-terminal glycine-glycine motif. Here, we report the solution structure of SAMP1 from Methanosarcina acetivorans and the activation of SAMPs by an archaeal protein with homology to eukaryotic E1 enzymes. Our results show that SAMP1 possesses a β-grasp fold and that its hydrophobic and electrostatic surface features are similar to those of MoaD. M. acetivorans SAMP1 exhibits an extensive flexible surface loop between helix-2 and the third strand of the β-sheet, which contributes to an elongated surface groove that is not observed in bacterial ubiquitin homologues and many other SAMPs. We provide in vitro biochemical evidence that SAMPs are activated in an ATP-dependent manner by an E1-like enzyme that we have termed E1-like SAMP activator (ELSA). We show that activation occurs by formation of a mixed anhydride (adenylate) at the SAMP C-terminus and is detectable by SDS-PAGE and electrospray ionization mass spectrometry.

PubMed: 21112336
DOI: 10.1016/j.jmb.2010.11.040

実験手法

SOLUTION NMR