Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 A

被引:109
作者
Gruswitz, Franz [1 ]
O'Connell, Joseph, III [1 ]
Stroud, Robert M. [1 ]
机构
[1] Univ Calif San Francisco, Sch Med, Dept Biochem & Biophys, San Francisco, CA 94143 USA
关键词
membrane; regulation; structure; allosteric; dinucleotide;
D O I
10.1073/pnas.0609796104
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Ammonia conductance is highly regulated. A P-parallel to signal transduction protein, GInK, is the final regulator of transmembrane ammonia conductance by the ammonia channel AmtB in Escherichia coli. The complex formed between AmtB and inhibitory GInK at 1.96-angstrom resolution shows that the trimeric channel is blocked directly by GInK and how, in response to intracellular nitrogen status, the ability of GInK to block the channel is regulated by uridylylation/ deuridylylation at Y51. ATP and Mg2+ augment the interaction of GlnK. The hydrolyzed product, adenosine 5'-diphosphate orients the surface of GInK for AmtB blockade. 2-Oxoglutarate diminishes AmtB/GInK association, and sites for 2-oxoglutarate are evaluated.
引用
收藏
页码:42 / 47
页数:6
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