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| - | [[Image:1hwy.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1hwy.png|left|200px]] |
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| | {{STRUCTURE_1hwy| PDB=1hwy | SCENE= }} | | {{STRUCTURE_1hwy| PDB=1hwy | SCENE= }} |
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| - | '''BOVINE GLUTAMATE DEHYDROGENASE COMPLEXED WITH NAD AND 2-OXOGLUTARATE'''
| + | ===BOVINE GLUTAMATE DEHYDROGENASE COMPLEXED WITH NAD AND 2-OXOGLUTARATE=== |
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| - | ==Overview==
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| - | Glutamate dehydrogenase is found in all organisms and catalyses the oxidative deamination of l-glutamate to 2-oxoglutarate. However, only animal GDH utilizes both NAD(H) or NADP(H) with comparable efficacy and exhibits a complex pattern of allosteric inhibition by a wide variety of small molecules. The major allosteric inhibitors are GTP and NADH and the two main allosteric activators are ADP and NAD(+). The structures presented here have refined and modified the previous structural model of allosteric regulation inferred from the original boGDH.NADH.GLU.GTP complex. The boGDH.NAD(+).alpha-KG complex structure clearly demonstrates that the second coenzyme-binding site lies directly under the "pivot helix" of the NAD(+) binding domain. In this complex, phosphates are observed to occupy the inhibitory GTP site and may be responsible for the previously observed structural stabilization by polyanions. The boGDH.NADPH.GLU.GTP complex shows the location of the additional phosphate on the active site coenzyme molecule and the GTP molecule bound to the GTP inhibitory site. As expected, since NADPH does not bind well to the second coenzyme site, no evidence of a bound molecule is observed at the second coenzyme site under the pivot helix. Therefore, these results suggest that the inhibitory GTP site is as previously identified. However, ADP, NAD(+), and NADH all bind under the pivot helix, but a second GTP molecule does not. Kinetic analysis of a hyperinsulinism/hyperammonemia mutant strongly suggests that ATP can inhibit the reaction by binding to the GTP site. Finally, the fact that NADH, NAD(+), and ADP all bind to the same site requires a re-analysis of the previous models for NADH inhibition.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11254391}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11254391 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11254391}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Glutamate dehydrogenase]] | | [[Category: Glutamate dehydrogenase]] |
| | [[Category: Nad]] | | [[Category: Nad]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:18:37 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:02:47 2008'' |
Revision as of 07:02, 1 July 2008
Template:STRUCTURE 1hwy
BOVINE GLUTAMATE DEHYDROGENASE COMPLEXED WITH NAD AND 2-OXOGLUTARATE
Template:ABSTRACT PUBMED 11254391
About this Structure
1HWY is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation., Smith TJ, Peterson PE, Schmidt T, Fang J, Stanley CA, J Mol Biol. 2001 Mar 23;307(2):707-20. PMID:11254391
Page seeded by OCA on Tue Jul 1 10:02:47 2008
