2agm: Difference between revisions
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[[Image:2agm.gif|left|200px]] | [[Image:2agm.gif|left|200px]] | ||
'''Solution structure of the R-module from AlgE4''' | {{Structure | ||
|PDB= 2agm |SIZE=350|CAPTION= <scene name='initialview01'>2agm</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= R-module subunit from algE4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 Azotobacter vinelandii]) | |||
}} | |||
'''Solution structure of the R-module from AlgE4''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2AGM is a [ | 2AGM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGM OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16407237 16407237] | ||
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: parallel beta-roll]] | [[Category: parallel beta-roll]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:49:28 2008'' | ||
Revision as of 13:49, 20 March 2008
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| Gene: | R-module subunit from algE4 (Azotobacter vinelandii) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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