This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2d43

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2d43.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2d43.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2d43| PDB=2d43 | SCENE= }}
{{STRUCTURE_2d43| PDB=2d43 | SCENE= }}
-
'''Crystal structure of arabinofuranosidase complexed with arabinotriose'''
+
===Crystal structure of arabinofuranosidase complexed with arabinotriose===
-
==Overview==
+
<!--
-
Alpha-L-arabinofuranosidase catalyses the hydrolysis of the alpha-1,2-, alpha-1,3-, and alpha-1,5-L-arabinofuranosidic bonds in L-arabinose-containing hemicelluloses such as arabinoxylan. AkAbf54 (the glycoside hydrolase family 54 alpha-L-arabinofuranosidase from Aspergillus kawachii) consists of two domains, a catalytic and an arabinose-binding domain. The latter has been named AkCBM42 [family 42 CBM (carbohydrate-binding module) of AkAbf54] because homologous domains are classified into CBM family 42. In the complex between AkAbf54 and arabinofuranosyl-alpha-1,2-xylobiose, the arabinose moiety occupies the binding pocket of AkCBM42, whereas the xylobiose moiety is exposed to the solvent. AkCBM42 was found to facilitate the hydrolysis of insoluble arabinoxylan, because mutants at the arabinose binding site exhibited markedly decreased activity. The results of binding assays and affinity gel electrophoresis showed that AkCBM42 interacts with arabinose-substituted, but not with unsubstituted, hemicelluloses. Isothermal titration calorimetry and frontal affinity chromatography analyses showed that the association constant of AkCBM42 with the arabinose moiety is approximately 10(3) M(-1). These results indicate that AkCBM42 binds the non-reducing-end arabinofuranosidic moiety of hemicellulose. To our knowledge, this is the first example of a CBM that can specifically recognize the side-chain monosaccharides of branched hemicelluloses.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16846393}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16846393 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16846393}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Wakagi, T.]]
[[Category: Wakagi, T.]]
[[Category: Arabinotriose complex]]
[[Category: Arabinotriose complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:40:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:19:43 2008''

Revision as of 13:19, 28 July 2008

Image:2d43.png

Template:STRUCTURE 2d43

Crystal structure of arabinofuranosidase complexed with arabinotriose

Template:ABSTRACT PUBMED 16846393

About this Structure

2D43 is a Single protein structure of sequence from Aspergillus kawachii. Full crystallographic information is available from OCA.

Reference

The family 42 carbohydrate-binding module of family 54 alpha-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose., Miyanaga A, Koseki T, Miwa Y, Mese Y, Nakamura S, Kuno A, Hirabayashi J, Matsuzawa H, Wakagi T, Shoun H, Fushinobu S, Biochem J. 2006 Nov 1;399(3):503-11. PMID:16846393

Page seeded by OCA on Mon Jul 28 16:19:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d43"
Personal tools