1ea0
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(New page: 200px<br /> <applet load="1ea0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ea0, resolution 3.0Å" /> '''ALPHA SUBUNIT OF A. ...)
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Revision as of 15:26, 29 October 2007
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ALPHA SUBUNIT OF A. BRASILENSE GLUTAMATE SYNTHASE
Overview
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 ... [(full description)]
About this Structure
1EA0 is a [Single protein] structure of sequence from [Azospirillum brasilense] with OMT, FMN, AKG and F3S as [ligands]. Active as [[1]], with EC number [1.4.1.13]. 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
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