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.


1mvy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mvy.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1mvy.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mvy| PDB=1mvy | SCENE= }}
{{STRUCTURE_1mvy| PDB=1mvy | SCENE= }}
-
'''Amylosucrase mutant E328Q co-crystallized with maltoheptaose.'''
+
===Amylosucrase mutant E328Q co-crystallized with maltoheptaose.===
-
==Overview==
+
<!--
-
The glucosyltransferase amylosucrase is structurally quite similar to the hydrolase alpha-amylase. How this switch in functionality is achieved is an important and fundamental question. The inactive E328Q amylosucrase variant has been co-crystallized with maltoheptaose, and the structure was determined by x-ray crystallography to 2.2 A resolution, revealing a maltoheptaose binding site in the B'-domain somewhat distant from the active site. Additional soaking of these crystals with maltoheptaose resulted in replacement of Tris in the active site with maltoheptaose, allowing the mapping of the -1 to +5 binding subsites. Crystals of amylosucrase were soaked with sucrose at different concentrations. The structures at approximately 2.1 A resolution revealed three new binding sites of different affinity. The highest affinity binding site is close to the active site but is not in the previously identified substrate access channel. Allosteric regulation seems necessary to facilitate access from this binding site. The structures show the pivotal role of the B'-domain in the transferase reaction. Based on these observations, an extension of the hydrolase reaction mechanism valid for this enzyme can be proposed. In this mechanism, the glycogen-like polymer is bound in the widest access channel to the active site. The polymer binding introduces structural changes that allow sucrose to migrate from its binding site into the active site and displace the polymer.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12364331}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12364331 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12364331}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Sprogoe, D.]]
[[Category: Sprogoe, D.]]
[[Category: Protein-sugar complex]]
[[Category: Protein-sugar complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:47:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:21:40 2008''

Revision as of 06:21, 28 July 2008

Image:1mvy.png

Template:STRUCTURE 1mvy

Amylosucrase mutant E328Q co-crystallized with maltoheptaose.

Template:ABSTRACT PUBMED 12364331

About this Structure

1MVY is a Single protein structure of sequence from Neisseria polysaccharea. Full crystallographic information is available from OCA.

Reference

Oligosaccharide and sucrose complexes of amylosucrase. Structural implications for the polymerase activity., Skov LK, Mirza O, Sprogoe D, Dar I, Remaud-Simeon M, Albenne C, Monsan P, Gajhede M, J Biol Chem. 2002 Dec 6;277(49):47741-7. Epub 2002 Oct 2. PMID:12364331

Page seeded by OCA on Mon Jul 28 09:21:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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