Cryo-EM Structure of a Molluscan Hemocyanin Suggests Its Allosteric Mechanism
文献类型：期刊论文
| 作者 | Zhang, QF; Dai, XH; Cong, Y; Zhang, JJ; Chen, DH; Dougherty, MT; Wang, JY; Ludtke, SJ; Schmid, MF; Chiu, W |
| 刊名 | STRUCTURE
 |
| 出版日期 | 2013 |
| 卷号 | 21期号:4页码:604-613 |
| 通讯作者 | Chiu, W (reprint author), Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Natl Ctr Macromol Imaging, Houston, TX 77030 USA.,wah@bcm.edu |
| 英文摘要 | Hemocyanins are responsible for transporting O-2 in the arthropod and molluscan hemolymph. Haliotis diversicolor molluscan hemocyanin isoform 1 (HdH1) is an 8 MDa oligomer. Each subunit is made up of eight functional units (FUs). Each FU contains two Cu ions, which can reversibly bind an oxygen molecule. Here, we report a 4.5 angstrom cryo-EM structure of HdH1. The structure clearly shows ten asymmetric units arranged with D5 symmetry. Each asymmetric unit contains two structurally distinct but chemically identical subunits. The map is sufficiently resolved to trace the entire subunit C alpha backbone and to visualize densities corresponding to some large side chains, Cu ion pairs, and interaction networks of adjacent subunits. A FU topology path intertwining between the two subunits of the asymmetric unit is unambiguously determined. Our observations suggest a structural mechanism for the stability of the entire hemocyanin didecamer and 20 "communication clusters" across asymmetric units responsible for its allosteric property upon oxygen binding. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| 关键词[WOS] | PARTICLE ELECTRON CRYOMICROSCOPY ; POMATIA ALPHA-HEMOCYANIN ; FUNCTIONAL UNITS ; MOLECULAR-MODEL ; PLUS QS21 ; MICROSCOPY ; EVOLUTION ; SUBUNIT ; RECONSTRUCTION ; PROTEIN |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000317800100010 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/374]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Zhang, QF,Dai, XH,Cong, Y,et al. Cryo-EM Structure of a Molluscan Hemocyanin Suggests Its Allosteric Mechanism[J]. STRUCTURE,2013,21(4):604-613. |
| APA | Zhang, QF.,Dai, XH.,Cong, Y.,Zhang, JJ.,Chen, DH.,...&Chiu, W.(2013).Cryo-EM Structure of a Molluscan Hemocyanin Suggests Its Allosteric Mechanism.STRUCTURE,21(4),604-613. |
| MLA | Zhang, QF,et al."Cryo-EM Structure of a Molluscan Hemocyanin Suggests Its Allosteric Mechanism".STRUCTURE 21.4(2013):604-613. |
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