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结核分枝杆菌磷酸泛酰巯基乙胺腺苷酰转移酶与反馈抑制剂辅酶A复合物的结构仅揭示了一种活性位点构象。

Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation.

作者信息

Wubben T, Mesecar A D

机构信息

Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois, USA.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):541-5. doi: 10.1107/S1744309111010761. Epub 2011 Apr 20.

Abstract

Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in the coenzyme A (CoA) biosynthetic pathway, reversibly transferring an adenylyl group from ATP to 4'-phosphopantetheine to form dephosphocoenzyme A (dPCoA). To complement recent biochemical and structural studies on Mycobacterium tuberculosis PPAT (MtPPAT) and to provide further insight into the feedback regulation of MtPPAT by CoA, the X-ray crystal structure of the MtPPAT enzyme in complex with CoA was determined to 2.11 Å resolution. Unlike previous X-ray crystal structures of PPAT-CoA complexes from other bacteria, which showed two distinct CoA conformations bound to the active site, only one conformation of CoA is observed in the MtPPAT-CoA complex.

摘要

磷酸泛酰巯基乙胺腺苷酰转移酶(PPAT)催化辅酶A(CoA)生物合成途径中的倒数第二步反应,可逆地将腺苷酰基从ATP转移至4'-磷酸泛酰巯基乙胺,形成脱磷酸辅酶A(dPCoA)。为补充近期关于结核分枝杆菌PPAT(MtPPAT)的生化和结构研究,并进一步深入了解CoA对MtPPAT的反馈调节,测定了与CoA结合的MtPPAT酶的X射线晶体结构,分辨率为2.11 Å。与之前其他细菌的PPAT-CoA复合物的X射线晶体结构不同,后者显示有两种不同的CoA构象与活性位点结合,而在MtPPAT-CoA复合物中仅观察到一种CoA构象。

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