User:Cameron Evans/Sandbox 1

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	===General Structure===		===General Structure===
-		+	Unlike the prokaryotic GluDH, mammalian GluDH has been found to always hexamerize as a dimer of
		+	<scene name='User:Cameron_Evans/Sandbox_1/Human_d_e_f/1'>trimers</scene>. Also unlike prokaryotic GluDH, the <scene name='User:Cameron_Evans/Sandbox_1/Human_d_alone/1'>monomer</scene> has 48 residue "antenna" that assists in the trimerization process. <scene name='User:Cameron_Evans/Sandbox_1/Human_d_e_f/1'>(The interactions of the antennae are best seen in the trimer)</scene>. These antennae appear to undergo conformational changes as the "mouth" of GluDH opens and closes (see morph below).
	===Specificity===		===Specificity===
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	===Allosteric Interactions===		===Allosteric Interactions===
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-	<scene name='User:Cameron_Evans/Sandbox_1/Human_d_e_f/1'>Trimer (1/2 of GDH)</scene>
-
-	<scene name='User:Cameron_Evans/Sandbox_1/Human_d_alone/1'>Monomer</scene>
	==References==		==References==
	----		----
	<references />		<references />

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Revision as of 22:44, 3 April 2010

Glutamate Dehydrogenase

Contents 1 Prokaryote 1.1 General Structure 1.2 Specificity 1.3 Allosteric Interactions 2 Eukaryote 2.1 General Structure 2.2 Specificity 2.3 Allosteric Interactions 3 References

Prokaryote

spinqualitylabelsall models PDB ID 1bgv Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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.

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Domain II is in Blue and Domain I is in Purple

Allosteric Interactions

m m m m

...more to come

Eukaryote

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

General Structure

Unlike the prokaryotic GluDH, mammalian GluDH has been found to always hexamerize as a dimer of . Also unlike prokaryotic GluDH, the has 48 residue "antenna" that assists in the trimerization process. . These antennae appear to undergo conformational changes as the "mouth" of GluDH opens and closes (see morph below).

Specificity

Allosteric Interactions

References

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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