在真核生物和原核生物中 B12 结合蛋白的晶体学研究。
Crystallographic studies on B12 binding proteins in eukaryotes and prokaryotes.
机构信息
NE-CAT and Department of Chemistry and Chemical Biology, Cornell University, Building 436E, Argonne National Laboratory, Argonne, IL 60439, USA.
出版信息
Biochimie. 2013 May;95(5):976-88. doi: 10.1016/j.biochi.2013.01.014. Epub 2013 Feb 5.
Abstract
The X-ray crystal structures of several important vitamin B12 binding proteins that have been solved in recent years have enhanced our current understanding in the vitamin B12 field. These structurally diverse groups of B12 binding proteins perform various important biological activities, both by transporting B12 as well as catalyzing various biological reactions. An in-depth comparative analysis of these structures was carried out using PDB coordinates of a carefully chosen database of B12 binding proteins to correlate the overall folding of the molecule with phylogeny, the B12 interactions, and with their biological function. The structures of these proteins are discussed in the context of this comparative analysis.
摘要
近年来已经解决的几种重要维生素 B12 结合蛋白的 X 射线晶体结构提高了我们目前在维生素 B12 领域的认识。这些结构多样的 B12 结合蛋白群通过运输 B12 以及催化各种生物反应，执行着各种重要的生物活性。使用精心挑选的 B12 结合蛋白数据库的 PDB 坐标对这些结构进行了深入的比较分析，以将分子的整体折叠与系统发育、B12 相互作用以及它们的生物学功能相关联。本文将在比较分析的背景下讨论这些蛋白质的结构。
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