Department of Chemistry, University of Basel, Spitalstrasse 51, CH 4056-Basel, Switzerland.
Metallomics. 2012 Apr;4(4):379-88. doi: 10.1039/c2mt20010d. Epub 2012 Mar 5.
Among natural metalloenzymes, the facial two-histidines one-carboxylate binding motif (FTM) is a widely represented first coordination sphere motif present in the active site of a variety of metalloenzymes. A PDB search revealed a total of 1685 structures bearing such FTMs bound to a metal. Sixty statistically representative FTMs were selected and used as template for the identification of structurally characterized proteins bearing these three amino acids in a propitious environment for binding to a transition metal. This geometrical superposition search, carried out using the STAMPS software, returned 2320 hits. While most consisted of either apo-FTMs or bore strong sequence homology to known FTMs, seven such structures lying within a cavity were identified as novel and viable scaffolds for the creation of artificial metalloenzymes bearing an FTM.
在天然金属酶中，面两个组氨酸一个羧酸结合基序（FTM）是一个广泛存在的第一配位球基序，存在于各种金属酶的活性位点中。PDB 搜索共显示了 1685 个结构，这些结构带有这种 FTM，与金属结合。选择了 60 个具有统计学代表性的 FTM，并将其用作模板，用于识别在有利于与过渡金属结合的有利环境中具有这三个氨基酸的结构特征蛋白。使用 STAMPS 软件进行的这种几何叠加搜索，返回了 2320 个命中。虽然大多数命中结构要么是无配体的 FTM，要么与已知的 FTM 具有强烈的序列同源性，但在一个腔体内发现了七个这样的结构，它们被鉴定为具有 FTM 的人工金属酶的新的可行支架。
