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.


2qqu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_2qqu", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:2qqu.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2qqu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qqu| PDB=2qqu | SCENE= }}
{{STRUCTURE_2qqu| PDB=2qqu | SCENE= }}
-
'''Crystal structure of a cell-wall invertase (D239A) from Arabidopsis thaliana in complex with sucrose'''
+
===Crystal structure of a cell-wall invertase (D239A) from Arabidopsis thaliana in complex with sucrose===
-
==Overview==
+
<!--
-
In plants, cell-wall invertases fulfil important roles in carbohydrate partitioning, growth, development and crop yield. In this study, we report on different X-ray crystal structures of Arabidopsis thaliana cell-wall invertase 1 (AtcwINV1) mutants with sucrose. These structures reveal a detailed view of sucrose binding in the active site of the wild-type AtcwINV1. Compared to related enzyme-sucrose complexes, important differences in the orientation of the glucose subunit could be observed. The structure of the E203Q AtcwINV1 mutant showed a complete new binding modus, whereas the D23A, E203A and D239A structures most likely represent the productive binding modus. Together with a hydrophobic zone formed by the conserved W20, W47 and W82, the residues N22, D23, R148, E203, D149 and D239 are necessary to create the ideal sucrose-binding pocket. D239 can interact directly with the glucose moiety of sucrose, whereas K242 has an indirect role in substrate stabilization. Most probably, K242 keeps D239 in a favourable position upon substrate binding. Unravelling the exact position of sucrose in plant cell-wall invertases is a necessary step towards the rational design of superior invertases to further increase crop yield and biomass production.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18258263}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18258263 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18258263}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Invertase]]
[[Category: Invertase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:41:30 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:37:33 2008''

Revision as of 15:37, 27 July 2008

Image:2qqu.png

Template:STRUCTURE 2qqu

Crystal structure of a cell-wall invertase (D239A) from Arabidopsis thaliana in complex with sucrose

Template:ABSTRACT PUBMED 18258263

About this Structure

2QQU is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose., Lammens W, Le Roy K, Van Laere A, Rabijns A, Van den Ende W, J Mol Biol. 2008 Mar 21;377(2):378-85. Epub 2008 Jan 5. PMID:18258263

Page seeded by OCA on Sun Jul 27 18:37:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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