Literature DB >> 17768346

Preliminary X-ray analysis of cellobiohydrolase Cel7B from Melanocarpus albomyces.

Tarja Parkkinen1, Anu Koivula, Jari Vehmaanperä, Juha Rouvinen.   

Abstract

Cellobiohydrolases are enzymes that cleave off cellobiose units from cellulose chains in a processive manner. Melanocarpus albomyces Cel7B is a thermostable single-module cellobiohydrolase that has relatively low activity on small soluble substrates at room temperature. It belongs to glycoside hydrolase family 7, which includes endo-beta-1,4-glucanases and cellobiohydrolases. Cel7B was crystallized using the hanging-drop vapour-diffusion method and streak-seeding. The crystals belonged to space group P2(1), with unit-cell parameters a = 50.9, b = 94.5, c = 189.8 A, beta = 90.0 degrees and four monomers in the asymmetric unit. Analysis of the intensity statistics showed that the crystals were pseudo-merohedrally twinned, with a twinning fraction of 0.37. X-ray diffraction data were collected at 1.6 A resolution using synchrotron radiation.

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Year:  2007        PMID: 17768346      PMCID: PMC2376320          DOI: 10.1107/S1744309107034458

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


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  2 in total

1.  Effect of pH and temperature on the global compactness, structure, and activity of cellobiohydrolase Cel7A from Trichoderma harzianum.

Authors:  Francieli Colussi; Wanius Garcia; Flávio Rodolfo Rosseto; Bruno Luan Soares de Mello; Mário de Oliveira Neto; Igor Polikarpov
Journal:  Eur Biophys J       Date:  2011-11-03       Impact factor: 1.733

2.  Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding.

Authors:  Tarja Parkkinen; Anu Koivula; Jari Vehmaanperä; Juha Rouvinen
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  2 in total

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