From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ofe.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ofe.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ofe| PDB=1ofe | SCENE= }} | | {{STRUCTURE_1ofe| PDB=1ofe | SCENE= }} |
| | | | |
| - | '''GLUTAMATE SYNTHASE FROM SYNECHOCYSTIS SP IN COMPLEX WITH 2-OXOGLUTARATE AND L-DON AT 2.45 ANGSTROM RESOLUTION'''
| + | ===GLUTAMATE SYNTHASE FROM SYNECHOCYSTIS SP IN COMPLEX WITH 2-OXOGLUTARATE AND L-DON AT 2.45 ANGSTROM RESOLUTION=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Glutamate synthases (GltS) are crucial enzymes in ammonia assimilation in plants and bacteria, where they catalyze the formation of two molecules of L-glutamate from L-glutamine and 2-oxoglutarate. The plant-type ferredoxin-dependent GltS and the functionally homologous alpha subunit of the bacterial NADPH-dependent GltS are complex four-domain monomeric enzymes of 140-165 kDa belonging to the NH(2)-terminal nucleophile family of amidotransferases. The enzymes function through the channeling of ammonia from the N-terminal amidotransferase domain to the FMN-binding domain. Here, we report the X-ray structure of the Synechocystis ferredoxin-dependent GltS with the substrate 2-oxoglutarate and the covalent inhibitor 5-oxo-L-norleucine bound in their physically distinct active sites solved using a new crystal form. The covalent Cys1-5-oxo-L-norleucine adduct mimics the glutamyl-thioester intermediate formed during L-glutamine hydrolysis. Moreover, we determined a high resolution structure of the GltS:2-oxoglutarate complex. These structures represent the enzyme in the active conformation. By comparing these structures with that of GltS alpha subunit and of related enzymes we propose a mechanism for enzyme self-regulation and ammonia channeling between the active sites. X-ray small-angle scattering experiments were performed on solutions containing GltS and its physiological electron donor ferredoxin (Fd). Using the structure of GltS and the newly determined crystal structure of Synechocystis Fd, the scattering experiments clearly showed that GltS forms an equimolar (1:1) complex with Fd. A fundamental consequence of this result is that two Fd molecules bind consecutively to Fd-GltS to yield the reduced FMN cofactor during catalysis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12818206}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12818206 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12818206}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| | [[Category: Substrate channeling]] | | [[Category: Substrate channeling]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:46:45 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:36:27 2008'' |
Revision as of 08:36, 29 July 2008
Template:STRUCTURE 1ofe
GLUTAMATE SYNTHASE FROM SYNECHOCYSTIS SP IN COMPLEX WITH 2-OXOGLUTARATE AND L-DON AT 2.45 ANGSTROM RESOLUTION
Template:ABSTRACT PUBMED 12818206
About this Structure
1OFE is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
Reference
The active conformation of glutamate synthase and its binding to ferredoxin., van den Heuvel RH, Svergun DI, Petoukhov MV, Coda A, Curti B, Ravasio S, Vanoni MA, Mattevi A, J Mol Biol. 2003 Jun 27;330(1):113-28. PMID:12818206
Page seeded by OCA on Tue Jul 29 11:36:27 2008
