Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP

被引：0
|
作者：
Jacob L W Morgan
Joshua T McNamara
Jochen Zimmer
机构：
[1] Center for Membrane Biology,Department of Molecular Physiology and Biological Physics
[2] University of Virginia,undefined
来源：
Nature Structural & Molecular Biology | 2014年 / 21卷
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摘要：
Cyclic di-GMP (c-di-GMP) regulates a number of bacterial processes, including synthesis of cellulose during biofilm formation. The PilZ domain from bacterial cellulose synthase BcsA–BcsB senses c-di-GMP and activates the enzyme. Now crystal structures of BcsA–BcsB along with functional analysis reveal that binding of c-di-GMP releases a conserved gating loop to allow substrate to enter the active site.
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页码：489 / 496
页数：7
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