Patel Kirti, Kumar Anil, Durani Susheel
Department of Chemistry, Indian Institute of Technology Bombay, Mumbai-400076, India.
Biochim Biophys Acta. 2007 Oct;1774(10):1247-53. doi: 10.1016/j.bbapap.2007.07.010. Epub 2007 Aug 8.
In a recent sequence-analysis study it was concluded that up to 10% of the human proteome could be comprised of zinc proteins, quite varied in the functional spread. The native structures of only few of the proteins are actually established. The elucidation of rest of the sequences of not just human but even other actively investigated genomes may benefit from knowledge of the structural consensus of the zinc-binding centers of the currently known zinc proteins. Nearly four hundred X-ray and NMR structures in the database of zinc-protein structures available as of April 2007 were investigated for geometry and conformation in the zinc-binding centers; separately for the structural and catalytic proteins and individually in the zinc centers coordinated to three and four amino-acid ligands. Enhanced cysteine involvement in agreement with the observation in human proteome has been detected in contrast with previous reports. Deviations from ideal coordination geometries are detected, possible underlying reasons are investigated, and correlations of geometry and conformation in zinc-coordination centers with protein function are established, providing possible benchmarks for putative zinc-binding patterns of the burgeoning genome data.
在最近的一项序列分析研究中得出结论，人类蛋白质组中高达10%可能由锌蛋白组成，其功能分布差异很大。实际上仅确定了少数蛋白质的天然结构。不仅对人类，而且对其他正在积极研究的基因组，其余序列的阐明可能受益于对当前已知锌蛋白的锌结合中心结构共识的了解。对截至2007年4月可获得的锌蛋白结构数据库中的近400个X射线和核磁共振结构进行了锌结合中心的几何形状和构象研究；分别针对结构蛋白和催化蛋白，并在与三个和四个氨基酸配体配位的锌中心单独进行研究。与之前的报告相比，已检测到半胱氨酸参与度增加，这与在人类蛋白质组中的观察结果一致。检测到与理想配位几何形状的偏差，研究了可能的潜在原因，并建立了锌配位中心的几何形状和构象与蛋白质功能的相关性，为新兴基因组数据的假定锌结合模式提供了可能的基准。
