1wl7: Difference between revisions

Revision as of 15:31, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1wl7.png

Template:STRUCTURE 1wl7

Structure of the thermostable arabinanaseStructure of the thermostable arabinanase

Template:ABSTRACT PUBMED 15944411

About this StructureAbout this Structure

1WL7 is a Single protein structure of sequence from Geobacillus thermodenitrificans. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3., Yamaguchi A, Tada T, Wada K, Nakaniwa T, Kitatani T, Sogabe Y, Takao M, Sakai T, Nishimura K, J Biochem. 2005 May;137(5):587-92. PMID:15944411

Page seeded by OCA on Sun Jul 27 15:31:41 2008

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OCA

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-'''Structure of the thermostable arabinanase'''
+===Structure of the thermostable arabinanase===
-==Overview==
+<!--
-The crystal structure of a thermostable endo-1,5-alpha-L-arabinanase, ABN-TS, from Bacillus thermodenitrificans TS-3 was determined at 1.9 A to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed beta-propeller fold. The substrate-binding cleft formed across one face of the propeller is open on both sides to allow random binding of several sugar units in the polymeric substrate arabinan. The beta-propeller fold is stabilized through a ring closure. ABN-TS exhibits a new closure-mode involving residues in the N-terminal region: Phe7 to Gly21 exhibit hydrogen bonds and hydrophobic interactions with the first and last blades, and Phe4 links the second and third blades through a hydrogen bond and an aromatic stacking interaction, respectively. The role of the N-terminal region in the thermostability was confirmed with a mutant lacking 16 amino acid residues from the N-terminus of ABN-TS.
+The line below this paragraph, {{ABSTRACT_PUBMED_15944411}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15944411 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15944411}}
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 [[Category: Glycoside hydrolase]]
 [[Category: Thermostable enzyme]]
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