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-Structure paper
タイトル | The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly. |
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ジャーナル・号・ページ | Structure, Vol. 27, Issue 5, Page 749-763.e4, Year 2019 |
掲載日 | 2019年5月7日 |
著者 | Basil J Greber / Markus Sutter / Cheryl A Kerfeld / |
PubMed 要旨 | Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive ...Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive competitive advantages from their BMC-based catabolism, implicating BMCs as drug targets. BMC shells are of interest for bioengineering due to their diverse and selective permeability properties and because they self-assemble. A complete understanding of shell composition and organization is a prerequisite for biotechnological applications. Here, we report the cryoelectron microscopy structure of a BMC shell at 3.0-Å resolution, using an image-processing strategy that allowed us to determine the previously uncharacterized structural details of the interactions formed by the BMC-T and BMC-T shell subunits in the context of the assembled shell. We found unexpected structural plasticity among these interactions, resulting in distinct shell populations assembled from varying numbers of the BMC-T and BMC-T subunits. We discuss the implications of these findings on shell assembly and function. |
リンク | Structure / PubMed:30833088 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.0 - 4.4 Å |
構造データ | EMDB-9296: EMDB-9307: Structure of the HO BMC shell: BMC-TD focused structure, closed state EMDB-9308, PDB-6mzv: EMDB-9309, PDB-6mzx: EMDB-9310, PDB-6mzy: EMDB-9311, PDB-6n06: EMDB-9312, PDB-6n07: EMDB-9313, PDB-6n09: |
由来 |
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キーワード | STRUCTURAL PROTEIN (タンパク質) / microcompartment / shell / compartmentalization / BMC fold / VIRUS LIKE PARTICLE (ウイルス様粒子) |