2bkk

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spinqualitylabelsall models 2bkk, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF AMINOGLYCOSIDE PHOSPHOTRANSFERASE APH (3')-IIIA IN COMPLEX WITH THE INHIBITOR AR_3A

Overview

Aminoglycoside phosphotransferase (3')-IIIa (APH) is a bacterial kinase, that confers antibiotic resistance to many pathogenic bacteria and shares, structural homology with eukaryotic protein kinases. We report here the, crystal structure of APH, trapped in an inactive conformation by a, tailor-made inhibitory ankyrin repeat (AR) protein, at 2.15 A resolution., The inhibitor was selected from a combinatorial library of designed AR, proteins. The AR protein binds the C-terminal lobe of APH and thereby, stabilizes three alpha helices, which are necessary for substrate binding, in a significantly displaced conformation. BIAcore analysis and kinetic, enzyme inhibition experiments are consistent with the proposed allosteric, inhibition mechanism. In contrast to most small-molecule kinase, ... [(full description)]

About this Structure

2BKK is a [Protein complex] structure of sequences from [Enterococcus faecalis] with MG and ADP as [ligands]. Active as [[1]], with EC number [2.7.1.95]. Full crystallographic information is available from [OCA].

Reference

Allosteric inhibition of aminoglycoside phosphotransferase by a designed ankyrin repeat protein., Kohl A, Amstutz P, Parizek P, Binz HK, Briand C, Capitani G, Forrer P, Pluckthun A, Grutter MG, Structure. 2005 Aug;13(8):1131-41. PMID:16084385

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