1wky
From Proteopedia
Crystal structure of alkaline mannanase from Bacillus sp. strain JAMB-602: catalytic domain and its Carbohydrate Binding Module
Overview
An alkaline mannanase (EC 3.2.1.78) from the alkaliphilic Bacillus sp. strain JAMB-602 was cloned and sequenced. The deduced amino-acid sequence of the enzyme suggested that the enzyme consists of a catalytic and unknown additional domains. The recombinant enzyme expressed by B. subtilis was crystallized using the hanging-drop vapour-diffusion method at 277 K. X-ray diffraction data were collected to 1.65 A. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 70.7, b = 79.5, c = 80.4 A. The asymmetric unit contains one protein molecule, with a corresponding VM of 2.26 A3 Da(-1) and a solvent content of 45.6%. Molecular replacement for initial phasing was carried out using the three-dimensional structure of a mannanase from Thermomonospora fusca as a search model, which corresponds to the catalytic domain of the alkaline mannanase. It gave sufficient phases to build the unknown domain.
About this Structure
Full crystallographic information is available from OCA.
Reference
Crystallization and preliminary X-ray study of alkaline mannanase from an alkaliphilic Bacillus isolate., Akita M, Takeda N, Hirasawa K, Sakai H, Kawamoto M, Yamamoto M, Grant WD, Hatada Y, Ito S, Horikoshi K, Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1490-2. Epub 2004, Jul 21. PMID:15272186 Page seeded by OCA on Sat May 3 13:49:17 2008
