Molecular Insights of an Avian Species with Low Oxygen Affinity, the Crystal Structure of Duck T-State Methemoglobin

IF 1.9 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

The Protein Journal Pub Date : 2024-05-20 DOI:10.1007/s10930-024-10206-z

Sathya Moorthy Ponnuraj, Neelagandan Kamariah, Balasubramanian Moovarkumudalvan, Ramya Ramadoss, M. N. Ponnuswamy

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Abstract

Hemoglobin (Hb) is the key metalloprotein within red blood cells involved in oxygen transportation from lungs to body cells. The heme-iron atom inherent within Hb effectuates the mechanism of oxygen transportation and carbon dioxide removal. Structural investigations on avian Hb are limited when compared with the enormous work has been carried out on mammalian Hb. Here, the crystal structure of T-state methemoglobin (T-metHb) from domestic duck (Anas platyrhynchos), a low oxygen affinity avian species, determined to 2.1Å resolution is presented. Duck T-metHb crystallized in the orthorhombic space group C222₁ with unit cell parameters a = 59.89, b = 109.42 and c = 92.07Å. The final refined model with R-factor: 19.5% and R_free: 25.2% was obtained. The structural analysis reveals that duck T-metHb adopts a unique quaternary structure that is distinct from any of the avian liganded Hb structures. Moreover, it closely resembles the deoxy Hb of bar-headed goose, a high oxygen-affinity species. Besides the amino acid αPro119 located in the α1β1 interface, a unique quaternary structure with a constrained heme environment is attributed for the intrinsic low oxygen-affinity of duck Hb. This study reports the first protein crystal structure of low oxygen-affinity avian T-metHb from Anas platyrhynchos.

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对低氧亲和力禽类物种的分子认识--鸭 T 态高铁血红蛋白的晶体结构。

血红蛋白（Hb）是红细胞内的关键金属蛋白，参与从肺到身体细胞的氧气运输。Hb 中固有的血红素-铁原子实现了氧气运输和二氧化碳清除的机制。与哺乳动物 Hb 的大量研究工作相比，对鸟类 Hb 的结构研究十分有限。本文展示了家鸭（Anas platyrhynchos）这种低氧亲和力禽类的 T 态高铁血红蛋白（T-metHb）的晶体结构，其分辨率为 2.1 Å。鸭 T-metHb 在正交空间群 C2221 中结晶，单胞参数 a = 59.89、b = 109.42 和 c = 92.07 Å。最终得到的精炼模型的 R 因子为 19.5%，Rfree 为 25.2%：25.2%。结构分析表明，鸭 T-metHb 采用了独特的四元结构，不同于任何禽类配体 Hb 结构。此外，它与棒头鹅的脱氧 Hb（一种高氧亲和性物种）非常相似。除了位于α1β1界面的氨基酸αPro119外，鸭血红蛋白具有独特的四元结构和受约束的血红素环境，这也是鸭血红蛋白固有的低氧亲和性的原因。本研究首次报道了鸭血红蛋白（Anas platyrhynchos）的低亲氧性禽 T-metHb 蛋白晶体结构。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

The Protein Journal 生物-生化与分子生物学

CiteScore

5.20

自引率

0.00%

发文量

审稿时长

12 months

期刊介绍： The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.