2bw7

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spinqualitylabelsall models 2bw7, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

A NOVEL MECHANISM FOR ADENYLYL CYCLASE INHIBITION FROM THE CRYSTAL STRUCTURE OF ITS COMPLEX WITH CATECHOL ESTROGEN

Overview

Catechol estrogens are steroid metabolites that elicit physiological, responses through binding to a variety of cellular targets. We show here, that catechol estrogens directly inhibit soluble adenylyl cyclases and the, abundant trans-membrane adenylyl cyclases. Catechol estrogen inhibition is, non-competitive with respect to the substrate ATP, and we solved the, crystal structure of a catechol estrogen bound to a soluble adenylyl, cyclase from Spirulina platensis in complex with a substrate analog. The, catechol estrogen is bound to a newly identified, conserved hydrophobic, patch near the active center but distinct from the ATP-binding cleft., Inhibitor binding leads to a chelating interaction between the catechol, estrogen hydroxyl groups and the catalytic magnesium ion, distorting ... [(full description)]

About this Structure

2BW7 is a [Single protein] structure of sequence from [Spirulina platensis] with MG, CA, APC and ECS as [ligands]. Active as [[1]], with EC number [4.6.1.1]. Full crystallographic information is available from [OCA].

Reference

A novel mechanism for adenylyl cyclase inhibition from the crystal structure of its complex with catechol estrogen., Steegborn C, Litvin TN, Hess KC, Capper AB, Taussig R, Buck J, Levin LR, Wu H, J Biol Chem. 2005 Sep 9;280(36):31754-9. Epub 2005 Jul 7. PMID:16002394

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