User:Cameron Evans/Sandbox 1

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==Prokaryote==
==Prokaryote==
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<applet load='1bgv' size='300' frame='true' align='center' caption='GDH from ''Clostridium symbiosum'' ' />
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<applet load='1bgv' size='350' frame='true' align='Left' caption='GDH from ''Clostridium symbiosum'' ' />
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<center><scene name='User:Cameron_Evans/Sandbox_1/Reset/1'>RESET</scene></center>
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===General Structure===
===General Structure===
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The polar residues make specific contacts with the glutamine substrate.
The polar residues make specific contacts with the glutamine substrate.
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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' />
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<applet load='Temp.pdb' size='300' frame='true' align='right' scene='User:Cameron_Evans/Sandbox_1/Morph_side_view/1' target='0' />
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===Allosteric Interactions===
===Allosteric Interactions===
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...more to come
==Eukaryote==
==Eukaryote==

Revision as of 22:36, 3 April 2010

Glutamate Dehydrogenase

Contents

Prokaryote

PDB ID 1bgv

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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

...more to come

Eukaryote

Insert caption here

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General Structure

Specificity

Allosteric Interactions



References

  1. ↑ 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

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Cameron Evans

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