Majorek Karolina A, Gucwa Michal, Murzyn Krzysztof, Minor Wladek
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, United States.
Department of Computational Biophysics and Bioinformatics, Jagiellonian University, Krakow, Poland.
Front Chem. 2024 Aug 23;12:1426211. doi: 10.3389/fchem.2024.1426211. eCollection 2024.
Understanding the functions of metal ions in biological systems is crucial for many aspects of research, including deciphering their roles in diseases and potential therapeutic use. Structural information about the molecular or atomic details of these interactions, generated by methods like X-ray crystallography, cryo-electron microscopy, or nucleic magnetic resonance, frequently provides details that no other method can. As with any experimental method, they have inherent limitations that sometimes lead to an erroneous interpretation. This manuscript highlights different aspects of structural data available for metal-protein complexes. We examine the quality of modeling metal ion binding sites across different structure determination methods, where different kinds of errors stem from, and how they can impact correct interpretations and conclusions.
了解金属离子在生物系统中的功能对于许多研究领域都至关重要，包括解读它们在疾病中的作用以及潜在的治疗用途。通过X射线晶体学、冷冻电子显微镜或核磁共振等方法生成的关于这些相互作用的分子或原子细节的结构信息，常常能提供其他方法无法获得的详细信息。与任何实验方法一样，它们存在固有的局限性，有时会导致错误的解释。本手稿重点介绍了金属-蛋白质复合物可用结构数据的不同方面。我们研究了不同结构测定方法中金属离子结合位点建模的质量、不同类型错误的来源，以及它们如何影响正确的解释和结论。
