1hjs: Difference between revisions

Revision as of 08:17, 1 July 2008

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File:1hjs.png

Template:STRUCTURE 1hjs

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

Template:ABSTRACT PUBMED 12761390

About this StructureAbout this Structure

1HJS is a Single protein structure of sequence from Corynascus heterothallicus. 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

Page seeded by OCA on Tue Jul 1 08:16:59 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''STRUCTURE OF TWO FUNGAL BETA-1,4-GALACTANASES: SEARCHING FOR THE BASIS FOR TEMPERATURE AND PH OPTIMUM.'''
+===STRUCTURE OF TWO FUNGAL BETA-1,4-GALACTANASES: SEARCHING FOR THE BASIS FOR TEMPERATURE AND PH OPTIMUM.===
-==Overview==
+<!--
-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 active at acidic pH. The structure of the M. thermophila galactanase (MTGAL) was determined from crystals obtained with HEPES and TRIS buffers to 1.88 A and 2.14 A resolution, respectively. The structure of the H. insolens galactanase (HIGAL) was determined to 2.55 A resolution. The thermostability of MTGAL and HIGAL correlates with increase in the protein rigidity and electrostatic interactions, stabilization of the alpha-helices, and a tighter packing. An inspection of the active sites in the three enzymes identifies several amino acid substitutions that could explain the variation in pH optimum. Examination of the activity as a function of pH for the D182N mutant of AAGAL and the A90S/ H91D mutant of MTGAL showed that the difference in pH optimum between AAGAL and MTGAL is at least partially associated with differences in the nature of residues at positions 182, 90, and/or 91.
+The line below this paragraph, {{ABSTRACT_PUBMED_12761390}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12761390 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12761390}}
 ==About this Structure==
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 [[Category: Thermophile]]
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