1uzi

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spinqualitylabelsall models 1uzi, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

C3 EXOENZYME FROM CLOSTRIDIUM BOTULINUM, TETRAGONAL FORM

Overview

C3 exoenzyme from Clostridium botulinum (C3bot1) ADP-ribosylates and, thereby inactivates Rho A, B and C GTPases in mammalian cells. The, structure of a tetragonal crystal form has been determined by molecular, replacement and refined to 1.89 A resolution. It is very similar to the, apo structures determined previously from two different monoclinic crystal, forms. An objective reassessment of available apo and nucleotide-bound, C3bot1 structures indicates that, contrary to a previous report, the, protein possesses a rigid core formed largely of beta-strands and that the, general flexure that accompanies NAD binding is concentrated in two, peripheral lobes. Tetragonal crystals disintegrate in the presence of NAD, most likely because of disruption of essential crystal contacts.

About this Structure

1UZI is a [Single protein] structure of sequence from [Clostridium botulinum] with VO4, V4O and GOL as [ligands]. Active as [[1]], with EC number [2.4.2.30]. Full crystallographic information is available from [OCA].

Reference

C3 exoenzyme from Clostridium botulinum: structure of a tetragonal crystal form and a reassessment of NAD-induced flexure., Evans HR, Holloway DE, Sutton JM, Ayriss J, Shone CC, Acharya KR, Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1502-5. Epub 2004, Jul 21. PMID:15272191

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