3GFH
Crystal structure of EUTL shell protein of the bacterial ethanolamine micrompartment
3GFH の概要
| エントリーDOI | 10.2210/pdb3gfh/pdb |
| 関連するPDBエントリー | 3bn4 3cgi |
| 分子名称 | Ethanolamine utilization protein eutL, MERCURY (II) ION (3 entities in total) |
| 機能のキーワード | bacterial mircocompartment, shell protein, ethanolamine, structural protein |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 47668.49 |
| 構造登録者 | |
| 主引用文献 | Sagermann, M.,Ohtaki, A.,Nikolakakis, K. Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment Proc.Natl.Acad.Sci.USA, 106:8883-8887, 2009 Cited by PubMed Abstract: Bacterial microcompartments (BMCs) are specialized organelles that use proteinaceous membranes to confine chemical reaction spaces. The ethanolamine ammonialyase microcompartment of Escherichia coli represents such a class of cytosolic organelles that enables bacteria to survive on small organic molecules such as ethanolamine as the sole source for carbon and nitrogen. We present here the crystal structure of the shell protein EutL at 2.2-A resolution. With 219 residues, it is the largest representative of this BMC's shell proteins. In the crystal, EutL forms a trimer that exhibits a hexagonally shaped tile structure. The tiles arrange into a tightly packed 2D array that is likely to resemble the proteinaceous membrane of the intact BMC. In contrast to other BMC shell proteins, which have only 1 pore per tile, EutL exhibits 3 pores per tile, thereby significantly increasing the overall porosity of this protein membrane. Each of the individual pores is lined with negatively charged residues and aromatic residues that are proposed to facilitate passive transport of specific solutes. The characteristic shape of the hexagonal tile, which is also found in the microcompartments of carbon-fixating bacteria, may present an inherent and fundamental building unit that may provide a general explanation for the formation of differently sized microcompartments. PubMed: 19451619DOI: 10.1073/pnas.0902324106 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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