3U2H

Crystal structure of the C-terminal DUF1608 domain of the Methanosarcina acetivorans S-layer (MA0829) protein

3U2H の概要

• エントリーDOI: 10.2210/pdb3u2h/pdb
• 関連するPDBエントリー: 3U2G
• 分子名称: S-layer protein MA0829, GLYCEROL (3 entities in total)
• 機能のキーワード: duf1608 domain, cell envelop, surface layer, s-layer, unknown function, structural protein
• 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: 32200.68

構造登録者

Chan, S.,Phan, T.,Ahn, C.J.,Shin, A.,Rohlin, L.,Gunsalus, R.P.,Arbing, M.A. (登録日: 2011-10-03, 公開日: 2012-07-04, 最終更新日: 2023-09-13)

主引用文献

Arbing, M.A.,Chan, S.,Shin, A.,Phan, T.,Ahn, C.J.,Rohlin, L.,Gunsalus, R.P.
Structure of the surface layer of the methanogenic archaean Methanosarcina acetivorans.
Proc.Natl.Acad.Sci.USA, 109:11812-11817, 2012

PubMed Abstract: Archaea have a self-assembling proteinaceous surface (S-) layer as the primary and outermost boundary of their cell envelopes. The S-layer maintains structural rigidity, protects the organism from adverse environmental elements, and yet provides access to all essential nutrients. We have determined the crystal structure of one of the two "homologous" tandem polypeptide repeats that comprise the Methanosarcina acetivorans S-layer protein and propose a high-resolution model for a microbial S-layer. The molecular features of our hexameric S-layer model recapitulate those visualized by medium resolution electron microscopy studies of microbial S-layers and greatly expand our molecular view of S-layer dimensions, porosity, and symmetry. The S-layer model reveals a negatively charged molecular sieve that presents both a charge and size barrier to restrict access to the cell periplasmic-like space. The β-sandwich folds of the S-layer protein are structurally homologous to eukaryotic virus envelope proteins, suggesting that Archaea and viruses have arrived at a common solution for protective envelope structures. These results provide insight into the evolutionary origins of primitive cell envelope structures, of which the S-layer is considered to be among the most primitive: it also provides a platform for the development of self-assembling nanomaterials with diverse functional and structural properties.

PubMed: 22753492
DOI: 10.1073/pnas.1120595109

実験手法

X-RAY DIFFRACTION (2.36 Å)