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| - | [[Image:1ea0.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ea0| PDB=1ea0 | SCENE= }} | | {{STRUCTURE_1ea0| PDB=1ea0 | SCENE= }} |
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| - | '''ALPHA SUBUNIT OF A. BRASILENSE GLUTAMATE SYNTHASE'''
| + | ===ALPHA SUBUNIT OF A. BRASILENSE GLUTAMATE SYNTHASE=== |
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| - | ==Overview==
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| - | INTRODUCTION: The complex iron-sulfur flavoprotein glutamate synthase catalyses the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine, a reaction in the plant and bacterial pathway for ammonia assimilation. The enzyme functions through three distinct active centers carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor. RESULTS: The 3.0 A crystal structure of the dimeric 324 kDa core protein of a bacterial glutamate synthase was solved by the MAD method, using the very weak anomalous signal of the two 3Fe-4S clusters present in the asymmetric unit. The 1,472 amino acids of the monomer fold into a four-domain architecture. The two catalytic domains have canonical Ntn-amidotransferase and FMN binding (beta/alpha)8 barrel folds, respectively. The other two domains have an unusual "cut (beta/alpha)8 barrel" topology and an unexpected novel beta-helix structure. Channeling of the ammonia intermediate is brought about by an internal tunnel of 31 A length, which runs from the site of L-glutamine hydrolysis to the site of L-glutamate synthesis. CONCLUSIONS: The outstanding property of glutamate synthase is the ability to coordinate the activity of its various functional sites to avoid wasteful consumption of L-glutamine. The structure reveals two polypeptide segments that connect the catalytic centers and embed the ammonia tunnel, thus being ideally suited to function in interdomain signaling. Depending on the enzyme redox and ligation states, these signal-transducing elements may affect the active site geometry and control ammonia diffusion through a gating mechanism.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11188694}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11188694 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11188694}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Vanoni, M A.]] | | [[Category: Vanoni, M A.]] |
| | [[Category: Complex iron sulphur flavoprotein]] | | [[Category: Complex iron sulphur flavoprotein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:51:11 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:23:21 2008'' |
Revision as of 21:23, 30 June 2008
Template:STRUCTURE 1ea0
ALPHA SUBUNIT OF A. BRASILENSE GLUTAMATE SYNTHASE
Template:ABSTRACT PUBMED 11188694
About this Structure
1EA0 is a Single protein structure of sequence from Azospirillum brasilense. Full crystallographic information is available from OCA.
Reference
Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase., Binda C, Bossi RT, Wakatsuki S, Arzt S, Coda A, Curti B, Vanoni MA, Mattevi A, Structure. 2000 Dec 15;8(12):1299-308. PMID:11188694
Page seeded by OCA on Tue Jul 1 00:23:21 2008
