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Crystal structure and biophysical characterisation of Helicobacter pylori phosphopantetheine adenylyltransferase.

Abstract：

:Helicobacter pylori is a bacterium that causes chronic active gastritis and peptic ulcers. Drugs targeting H. pylori phosphopantetheine adenylyltransferase (HpPPAT), which is involved in CoA biosynthesis, may be useful. Herein, we report the expression in Escherichia coli and purification of recombinant HpPPAT and describe a crystal structure for an HpPPAT/CoA complex. As is the case for E. coli PPAT (EcPPAT), HpPPAT is hexameric in solution and as a crystal. Each protomer has a well-packed dinucleotide-binding fold in which CoA binds. Structural characterisation demonstrated that CoA derived from the E. coli expression system bound tightly to HpPPAT, presumably to initiate feedback inhibition. However, the interactions between the active-site residues of HpPPAT and CoA are not identical to those of other PPATs. Finally, CoA binding affects HpPPAT thermal denaturation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Cheng CS,Chen CH,Luo YC,Chen WT,Chang SY,Lyu PC,Kao MC,Yin HS

doi

10.1016/j.bbrc.2011.04.058

subject

Has Abstract

pub_date

2011-05-06 00:00:00

pages

356-61

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)00643-7

journal_volume

408

pub_type

杂志文章

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