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嗜热栖热菌中咪唑甘油磷酸(IGP)合酶蛋白HisF的1H、15N和13C共振归属

1H, 15N and 13C resonance assignment of imidazole glycerol phosphate (IGP) synthase protein HisF from Thermotoga maritima.

作者信息

Lipchock James M, Loria J Patrick

机构信息

Department of Chemistry, Yale University, Sterling Chemistry Laboratory, New Haven, CT, 06511, USA.

出版信息

Biomol NMR Assign. 2008 Dec;2(2):219-21. doi: 10.1007/s12104-008-9125-5. Epub 2008 Oct 7.

DOI:10.1007/s12104-008-9125-5
PMID:19636909
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2907236/
Abstract

HisF comprises one half of the heterodimeric protein complex imidazole glycerol phosphate (IGP) synthase responsible for the fifth step of histidine biosynthesis. Here we report backbone and side chain assignments necessary for characterization of protein dynamics involved in the allosteric mechanism of IGP synthase.

摘要

HisF是负责组氨酸生物合成第五步的异二聚体蛋白复合物咪唑甘油磷酸(IGP)合酶的一半。在此,我们报告了表征IGP合酶变构机制中涉及的蛋白质动力学所需的主链和侧链归属。

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1H, 15N and 13C resonance assignment of imidazole glycerol phosphate (IGP) synthase protein HisF from Thermotoga maritima.嗜热栖热菌中咪唑甘油磷酸(IGP)合酶蛋白HisF的1H、15N和13C共振归属
Biomol NMR Assign. 2008 Dec;2(2):219-21. doi: 10.1007/s12104-008-9125-5. Epub 2008 Oct 7.
2
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The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy.通过 NMR 光谱法检测氨和氙与海洋栖热菌咪唑甘油磷酸合酶的相互作用。
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Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex.来自嗜热栖热菌的咪唑甘油磷酸合酶。双酶复合物的四级结构、稳态动力学及反应机制。
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