title: Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis.
abstract: Xyn30D, a new member of a recently identified group of xylanases, has been purified and crystallized. Xyn30D is a bimodular enzyme composed of an N-terminal catalytic domain belonging to glycoside hydrolase family 30 (GH30) and a C-terminal family 35 carbohydrate-binding domain (CBM35) able to bind xylans and glucuronic acid. Xyn30D shares the characteristic endo mode of action described for GH30 xylanases, with the hydrolysis of the β-(1,4) bonds of xylan being directed by α-1,2-linked glucuronate moieties, which have to be placed at the -2 subsite of the xylanase active site. Crystals of the complete enzyme were obtained and a full data set to 2.3 Å resolution was collected using a synchrotron X-ray source. This represents the first bimodular enzyme with the domain architecture GH30-CBM35. This study will contribute to the understanding of the role that the different xylanases play in the depolymerization of glucuronoxylan.
authors.affiliation: Department of Crystallography and Structural Biology, Institute of Physical Chemistry `Rocasolano', Consejo Superior de Investigaciones Científicas, Serrano 119, 28006 Madrid, Spain.
authors.forename: María Ángela
authors.initials: MÁ
authors.lastname: Sainz-Polo
authors.affiliation: Department of Microbiology, Faculty of Biology, Universitat de Barcelona, Avenida Diagonal 643, 08028 Barcelona, Spain.
authors.forename: Susana Valeria
authors.initials: SV
authors.lastname: Valenzuela
authors.affiliation: Department of Microbiology, Faculty of Biology, Universitat de Barcelona, Avenida Diagonal 643, 08028 Barcelona, Spain.
authors.forename: F Javier
authors.initials: FJ
authors.lastname: Pastor
authors.affiliation: Department of Crystallography and Structural Biology, Institute of Physical Chemistry `Rocasolano', Consejo Superior de Investigaciones Científicas, Serrano 119, 28006 Madrid, Spain.
authors.forename: Julia
authors.initials: J
authors.lastname: Sanz-Aparicio
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D020723:Glucuronic Acid / Q000737:chemistry*; D056507:Paenibacillus / Q000737:chemistry* / Q000201:enzymology; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D014990:Xylans / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D014990:Xylans; D020723:Glucuronic Acid; D043364:Endo-1,4-beta Xylanases
keywords: CBM35; GH30; Paenibacillus barcinonensis; xylanase