Crystal structure of ubiquitin-like small archaeal modifier protein 1 (SAMP1) from Haloferax volcanii

Young Jee Jeong, Byung Cheon Jeong, Hyun Kyu Song

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The ubiquitin-like (Ubl) system has been shown to be ubiquitous in all three kingdoms of life following the very recent characterization of ubiquitin-like small archaeal modifier proteins (SAMP1 and 2) from Haloferax volcanii. The ubiquitin (Ub) and Ubl molecules in eukaryotes have been studied extensively and their cellular functions are well established. Biochemical and structural data pertaining to prokaryotic Ubl protein (Pup) continue to be reported. In contrast to eukaryotes and prokaryotes, no structural information on the archaeal Ubl molecule is available. Here we determined the crystal structure of SAMP1 at 1.55. Å resolution and generated a model of SAMP2. These were then compared with other Ubl molecules from eukaryotes as well as prokaryotes. The structure of SAMP1 shows a β-grasp fold of Ub, suggesting that the archaeal Ubl molecule is more closely related to eukaryotic Ub and Ubls than to its prokaryotic counterpart. The current structure identifies the location of critical elements such a single lysine residue (Lys4), C-terminal di-glycine motif, hydrophobic patches near leucine 60, and uniquely inserted α-helical segments (α1 and α3) in SAMP1. Based on the structure of SAMP1, several Ub-like features of SAMPs such as poly-SAMPylation and non-covalent interactions have been proposed, which should provide the basis for further investigations concerning the molecular function of archaeal Ubls and the large super-family of β-grasp fold proteins in the archaeal kingdom.

Original languageEnglish
Pages (from-to)112-117
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume405
Issue number1
DOIs
Publication statusPublished - 2011 Feb 4

Fingerprint

Haloferax volcanii
Archaeal Proteins
Ubiquitin
Crystal structure
Proteins
Eukaryota
Molecules
Ubiquitins
Hand Strength
Leucine
Glycine
Lysine

Keywords

  • β-Grasp fold
  • Archaea
  • Haloferax volcanii
  • Pup
  • SAMP1
  • SAMP2
  • Ubiquitin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Crystal structure of ubiquitin-like small archaeal modifier protein 1 (SAMP1) from Haloferax volcanii. / Jeong, Young Jee; Jeong, Byung Cheon; Song, Hyun Kyu.

In: Biochemical and Biophysical Research Communications, Vol. 405, No. 1, 04.02.2011, p. 112-117.

Research output: Contribution to journalArticle

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