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.


1y9g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1y9g.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1y9g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1y9g| PDB=1y9g | SCENE= }}
{{STRUCTURE_1y9g| PDB=1y9g | SCENE= }}
-
'''Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose'''
+
===Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose===
-
==Overview==
+
<!--
-
Exo-inulinases hydrolyze terminal, non-reducing 2,1-linked and 2,6-linked beta-d-fructofuranose residues in inulin, levan and sucrose releasing beta-d-fructose. We present the X-ray structure at 1.55A resolution of exo-inulinase from Aspergillus awamori, a member of glycoside hydrolase family 32, solved by single isomorphous replacement with the anomalous scattering method using the heavy-atom sites derived from a quick cryo-soaking technique. The tertiary structure of this enzyme folds into two domains: the N-terminal catalytic domain of an unusual five-bladed beta-propeller fold and the C-terminal domain folded into a beta-sandwich-like structure. Its structural architecture is very similar to that of another member of glycoside hydrolase family 32, invertase (beta-fructosidase) from Thermotoga maritima, determined recently by X-ray crystallography The exo-inulinase is a glycoprotein containing five N-linked oligosaccharides. Two crystal forms obtained under similar crystallization conditions differ by the degree of protein glycosylation. The X-ray structure of the enzyme:fructose complex, at a resolution of 1.87A, reveals two catalytically important residues: Asp41 and Glu241, a nucleophile and a catalytic acid/base, respectively. The distance between the side-chains of these residues is consistent with a double displacement mechanism of reaction. Asp189, which is part of the Arg-Asp-Pro motif, provides hydrogen bonds important for substrate recognition.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15522299}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15522299 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15522299}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Glycoside hydrolase family 32]]
[[Category: Glycoside hydrolase family 32]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:02:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:04:19 2008''

Revision as of 21:04, 28 July 2008

Image:1y9g.png

Template:STRUCTURE 1y9g

Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose

Template:ABSTRACT PUBMED 15522299

About this Structure

1Y9G is a Single protein structure of sequence from Aspergillus awamori. Full crystallographic information is available from OCA.

Reference

Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition., Nagem RA, Rojas AL, Golubev AM, Korneeva OS, Eneyskaya EV, Kulminskaya AA, Neustroev KN, Polikarpov I, J Mol Biol. 2004 Nov 19;344(2):471-80. PMID:15522299

Page seeded by OCA on Tue Jul 29 00:04:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y9g"
Personal tools