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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.
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Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.

机译：嗜热古细菌Sulfolobus solfataricus的3-磷酸甘油醛脱氢酶的晶体结构。

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摘要

The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaea shows low sequence identity (16-20%) with its eubacterial and eukaryotic counterparts. The crystal structure of the apo GAPDH from Sulfolobus solfataricus has been determined by multiple isomorphous replacement at 2.05 A resolution. The enzyme has several differences in secondary structure when compared with eubacterial GAPDHs, with an overall increase in the number of alpha-helices. There is a relocation of the active-site residues within the catalytic domain of the enzyme. The thermostability of the S. solfataricus enzyme can be attributed to a combination of an ion pair cluster and an intrasubunit disulphide bond. Copyright 1999 Academic Press.
机译：来自古细菌的酶甘油醛-3-磷酸脱氢酶（GAPDH）与它的真细菌和真核生物对应物显示出低序列同一性（16-20％）。来自Sulfolobus solfataricus的apo GAPDH的晶体结构已通过2.05 A分辨率的多个同构置换确定。与真细菌GAPDH相比，该酶的二级结构有几个差异，α-螺旋的总数总体上增加了。酶催化域内的活性位点残基发生重定位。啤酒酵母的热稳定性可以归因于离子对簇和亚单位内二硫键的组合。版权所有1999，学术出版社。

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