Structural dynamics and catalytic properties of a multi-modular xanthanase, native.
Structural dynamics and catalytic properties of a multi-modular xanthanase, native.
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DOI：
10.2210/pdb6fhj/pdb
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发表时间：
2018-05
期刊：
影响因子：
12.9
通讯作者：
O. Moroz;P. F. Jensen;S. P. McDonald;N. McGregor;E. Blagova;Gerard Comamala;D. Segura;Lars Anderson;S. M. Vasu;V. P. Rao;L. Giger;R. Monrad;A. Svendsen;J. Nielsen;B. Henrissat;G. Davies;H. Brumer;K. Rand;K. Wilson
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文献类型：
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作者：
O. Moroz;P. F. Jensen;S. P. McDonald;N. McGregor;E. Blagova;Gerard Comamala;D. Segura;Lars Anderson;S. M. Vasu;V. P. Rao;L. Giger;R. Monrad;A. Svendsen;J. Nielsen;B. Henrissat;G. Davies;H. Brumer;K. Rand;K. Wilson
用于分解复杂细菌多糖黄原胶的精确催化策略仍然是一个谜，黄原胶是人类加工食品中越来越常见的成分。在这里，我们提出了一个内切黄原胶酶的表征，从类芽孢杆菌南化。我们表明，它是一种CAZy家族9糖苷水解酶（GH 9），负责水解黄原胶主链，能够从多糖裂解酶家族8（PL 8）黄原胶裂解酶处理的黄原胶产生四聚体黄原胶寡糖。三维结构测定揭示了一种复杂的多模块酶，其中催化（α/α）6桶两侧是N-末端“免疫球蛋白样”（Ig样）结构域（常见于GH 9酶）和四个额外的C-末端全β折叠结构域，这些结构域在序列数据库中具有非常少的同源物，其中至少一个作为新的黄原胶结合结构域发挥作用，现在称为CBM 84。研究了该酶在天然钙包合物中的溶液相构象和动力学。
The precise catalytic strategies used for the breakdown of the complex bacterial polysaccharide xanthan, an increasingly frequent component of processed human foodstuffs, have remained a mystery. Here, we present characterization of an endo-xanthanase from Paenibacillus nanensis. We show that it is a CAZy family 9 glycoside hydrolase (GH9) responsible for the hydrolysis of the xanthan backbone capable of generating tetrameric xanthan oligosaccharides from polysaccharide lyase family 8 (PL8) xanthan lyase-treated xanthan. Three-dimensional structure determination reveals a complex multimodular enzyme in which a catalytic (α/α)6 barrel is flanked by an N-terminal “immunoglobulin-like” (Ig-like) domain (frequently found in GH9 enzymes) and by four additional C-terminal all β-sheet domains that have very few homologues in sequence databases and at least one of which functions as a new xanthan-binding domain, now termed CBM84. The solution-phase conformation and dynamics of the enzyme in the native calcium-bou...