2agm
From Proteopedia
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[[Image:2agm.gif|left|200px]] | [[Image:2agm.gif|left|200px]] | ||
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'''Solution structure of the R-module from AlgE4''' | '''Solution structure of the R-module from AlgE4''' | ||
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[[Category: Valla, S.]] | [[Category: Valla, S.]] | ||
[[Category: Wimmer, R.]] | [[Category: Wimmer, R.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:01:30 2008'' | |
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Revision as of 16:01, 3 May 2008
Solution structure of the R-module from AlgE4
Overview
In the bacterium Azotobacter vinelandii, a family of seven secreted and calcium-dependent mannuronan C-5 epimerases (AlgE1-7) has been identified. These epimerases are responsible for the epimerization of beta-d-mannuronic acid to alpha-l-guluronic acid in alginate polymers. The epimerases consist of two types of structural modules, designated A (one or two copies) and R (one to seven copies). The structure of the catalytically active A-module from the smallest epimerase AlgE4 (consisting of AR) has been solved recently. This paper describes the NMR structure of the R-module from AlgE4 and its titration with a substrate analogue and paramagnetic thulium ions. The R-module folds into a right-handed parallel beta-roll. The overall shape of the R-module is an elongated molecule with a positively charged patch that interacts with the substrate. Titration of the R-module with thulium indicated possible calcium binding sites in the loops formed by the nonarepeat sequences in the N-terminal part of the molecule and the importance of calcium binding for the stability of the R-module. Structure calculations showed that calcium ions can be incorporated in these loops without structural violations and changes. Based on the structure and the electrostatic surface potential of both the A- and R-module from AlgE4, a model for the appearance of the whole protein is proposed.
About this Structure
2AGM is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.
Reference
NMR structure of the R-module: a parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase., Aachmann FL, Svanem BI, Guntert P, Petersen SB, Valla S, Wimmer R, J Biol Chem. 2006 Mar 17;281(11):7350-6. Epub 2006 Jan 3. PMID:16407237 Page seeded by OCA on Sat May 3 19:01:30 2008
