1hjs

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Revision as of 20:22, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1hjs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hjs, resolution 1.87Å" /> '''STRUCTURE OF TWO FU...)
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File:1hjs.gif


1hjs, resolution 1.87Å

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STRUCTURE OF TWO FUNGAL BETA-1,4-GALACTANASES: SEARCHING FOR THE BASIS FOR TEMPERATURE AND PH OPTIMUM.

OverviewOverview

beta-1,4-Galactanases hydrolyze the galactan side chains that are part of, the complex carbohydrate structure of the pectin. They are assigned to, family 53 of the glycoside hydrolases and display significant variations, in their pH and temperature optimum and stability. Two fungal, beta-1,4-galactanases from Myceliophthora thermophila and Humicola, insolens have been cloned and heterologously expressed, and the crystal, structures of the gene products were determined. The structures are, compared to the previously only known family 53 structure of the, galactanase from Aspergillus aculeatus (AAGAL) showing approximately 56%, identity. The M. thermophila and H. insolens galactanases are thermophilic, enzymes and are most active at neutral to basic pH, whereas AAGAL is, mesophilic and most ... [(full description)]

About this StructureAbout this Structure

1HJS is a [Single protein] structure of sequence from [Thielavia heterothallica] with NAG, SO4, EPE and PEG as [ligands]. Active as [[1]], with EC number [3.2.1.89]. Full crystallographic information is available from [OCA].

ReferenceReference

Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum., Le Nours J, Ryttersgaard C, Lo Leggio L, Ostergaard PR, Borchert TV, Christensen LL, Larsen S, Protein Sci. 2003 Jun;12(6):1195-204. PMID:12761390

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