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.


1fhl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fhl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fhl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fhl| PDB=1fhl | SCENE= }}
{{STRUCTURE_1fhl| PDB=1fhl | SCENE= }}
-
'''CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 293K'''
+
===CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 293K===
-
==Overview==
+
<!--
-
The three-dimensional structure of Aspergillus aculeatus beta-1,4-galactanase (AAGAL), an enzyme involved in pectin degradation, has been determined by multiple isomorphous replacement to 2.3 and 1.8 A resolution at 293 and 100 K, respectively. It represents the first known structure for a polysaccharidase with this specificity and for a member of glycoside hydrolase family 53 (GH-53). The enzyme folds into a (beta/alpha)(8) barrel with the active site cleft located at the C-terminal side of the barrel consistent with the classification of GH-53 in clan GH-A, a superfamily of enzymes with common fold and catalytic machinery but diverse specificities. Putative substrate-enzyme interactions were elucidated by modeling of beta-1,4-linked galactobioses into the possible substrate binding subsites. The structure and modeling studies identified five potential subsites for the binding of galactans, of which one is a pocket suited for accommodating the arabinan side chain in arabinogalactan, one of the natural substrates. A comparison with the substrate binding grooves of other Clan GH-A enzymes suggests that shape complementarity is crucial in determining the specificity of polysaccharidases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12484750}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12484750 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12484750}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Family 53]]
[[Category: Family 53]]
[[Category: Glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:20:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:15:40 2008''

Revision as of 00:15, 1 July 2008

Template:STRUCTURE 1fhl

CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 293K

Template:ABSTRACT PUBMED 12484750

About this Structure

1FHL is a Single protein structure of sequence from Aspergillus aculeatus. Full crystallographic information is available from OCA.

Reference

Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A., Ryttersgaard C, Lo Leggio L, Coutinho PM, Henrissat B, Larsen S, Biochemistry. 2002 Dec 24;41(51):15135-43. PMID:12484750

Page seeded by OCA on Tue Jul 1 03:15:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools