User:Cameron Evans/Sandbox 1
From Proteopedia
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<applet load='Temp.pdb' size='300' frame='true' align='left' scene='User:Cameron_Evans/Sandbox_1/Morph_side_view/1' target='0' /> | <applet load='Temp.pdb' size='300' frame='true' align='left' scene='User:Cameron_Evans/Sandbox_1/Morph_side_view/1' target='0' /> | ||
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| + | <scene name='User:Cameron_Evans/Sandbox_1/Morph_side_view/2'>Side View</scene> | ||
| - | <scene name='User:Cameron_Evans/Sandbox_1/Morph_side_view/2'>Side View</scene> | ||
| + | <scene name='User:Cameron_Evans/Sandbox_1/Morph_side_view/1'>Top View</scene> | ||
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| - | <scene name='User:Cameron_Evans/Sandbox_1/Morph_side_view/1'>Top View</scene> | ||
===Allosteric Interactions=== | ===Allosteric Interactions=== | ||
Revision as of 22:33, 3 April 2010
Glutamate Dehydrogenase
Contents |
Prokaryote
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General Structure
Prokaryotic glutamate dehydrogenase (GDH) does not have any common quaternary structure among crystallized structures (1EUZ is a hexamer, 1HRD a trimer); however, every prokaryotic structure so far elucidated shows a common overall tertiary structure.[1]
Each monomer (reguardless of quaternary structure) has two domains: a domain that is a variant of the Rossmann dinucleotide binding fold (), and a domain involved in oligomerization (when it occurs) and contains most of the substrate binding residues (). [1]
Specificity
is made up of polar interactions from K89 and S380 and hydrophobic interactions from G90, V377 and A163. The last three residues that make this interaction are highly conserved among amino acid dehydrogenases. [1] The polar residues make specific contacts with the glutamine substrate.
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Domain II is in Blue and Domain I is in Purple
Allosteric Interactions
Eukaryote
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General Structure
Specificity
Allosteric Interactions
References
- ↑ 1.0 1.1 1.2 Stillman TJ, Baker PJ, Britton KL, Rice DW. Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J Mol Biol. 1993 Dec 20;234(4):1131-9. PMID:8263917 doi:http://dx.doi.org/10.1006/jmbi.1993.1665
