蛋白质亚单位
肽
化学
分子
三元络合物
丝氨酸
晶体结构
残留物(化学)
结晶学
蛋白激酶A
立体化学
三元运算
酶
生物化学
有机化学
基因
程序设计语言
计算机科学
作者
Jin Zheng,Elżbieta Anna Trafny,Daniel R. Knighton,Nguyen‐Huu Xuong,Susan S. Taylor,Lynn F. Ten Eyck,Janusz M. Sowadski
出处
期刊:Acta Crystallographica Section D-biological Crystallography
[International Union of Crystallography]
日期:1993-05-01
卷期号:49 (3): 362-365
被引量:319
标识
DOI:10.1107/s0907444993000423
摘要
. The crystal structure of a ternary complex containing the catalytic subunit of cAMP-dependent protein kinase, ATP and a 20-residue inhibitor peptide was refined at a resolution of 2.2 A to an R value of 0.177. In order to identify the metal binding sites, the crystals, originally grown in the presence of low concentrations of Mg(2+), were soaked in Mn(2+). Two Mn(2+) ions were identified using an anomalous Fourier map. One Mn(2+) ion bridges the gamma- and beta-phosphates and interacts with Asp184 and two water molecules. The second Mn(2+) ion interacts with the side chains of Asn171 and Asp l84 as well as with a water molecule. Modeling a serine into the P site of the inhibitor peptide suggests a mechanism for phosphotransfer.
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