Parker Siburt Claire J, Mietzner Timothy A, Crumbliss Alvin L
Department of Chemistry, Duke University, Durham, NC 27708-0346, USA.
Biochim Biophys Acta. 2012 Mar;1820(3):379-92. doi: 10.1016/j.bbagen.2011.09.001. Epub 2011 Sep 10.
Gram negative bacteria require iron for growth and virulence. It has been shown that certain pathogenic bacteria such as Neisseria gonorrhoeae possess a periplasmic protein called ferric binding protein (FbpA), which is a node in the transport of iron from the cell exterior to the cytosol.
The relevant literature is reviewed which establishes the molecular mechanism of FbpA mediated iron transport across the periplasm to the inner membrane.
Here we establish that FbpA may be considered a bacterial transferrin on structural and functional grounds. Data are presented which suggest a continuum whereby FbpA may be considered as a naked iron carrier, as well as a Fe-chelate carrier, and finally a member of the larger family of periplasmic binding proteins.
An investigation of the molecular mechanisms of action of FbpA as a member of the transferrin super family enhances our understanding of bacterial mechanisms for acquisition of the essential nutrient iron, as well as the modes of action of human transferrin, and may provide approaches to the control of pathogenic diseases. This article is part of a Special Issue entitled Transferrins: Molecular mechanisms of iron transport and disorders.
革兰氏阴性菌生长和致病需要铁。已表明某些病原菌如淋病奈瑟菌拥有一种称为铁结合蛋白（FbpA）的周质蛋白，它是铁从细胞外转运至胞质溶胶过程中的一个节点。
对相关文献进行综述，这些文献确立了FbpA介导铁跨周质转运至内膜的分子机制。
在此我们基于结构和功能依据确定FbpA可被视为一种细菌转铁蛋白。所呈现的数据表明存在一种连续统一体，据此FbpA可被视为一种裸铁载体、一种铁螯合物载体，最终是周质结合蛋白大家族的一员。
对FbpA作为转铁蛋白超家族成员的作用分子机制进行研究，可增进我们对细菌获取必需营养铁的机制以及人类转铁蛋白作用模式的理解，并可能提供控制致病疾病的方法。本文是名为“转铁蛋白：铁转运及紊乱的分子机制”的特刊的一部分。
