3k92

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Template:STRUCTURE 3k92

Contents

Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG

Template:ABSTRACT PUBMED 20630473

Function

[DHE2_BACSU] Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars.[1] [2] [3]

About this Structure

3k92 is a 6 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA.

See Also

Reference

  • Gunka K, Newman JA, Commichau FM, Herzberg C, Rodrigues C, Hewitt L, Lewis RJ, Stulke J. Functional dissection of a trigger enzyme: mutations of the bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties. J Mol Biol. 2010 Jul 23;400(4):815-27. Epub 2010 May 31. PMID:20630473 doi:10.1016/j.jmb.2010.05.055
  1. ↑ Belitsky BR, Sonenshein AL. Role and regulation of Bacillus subtilis glutamate dehydrogenase genes. J Bacteriol. 1998 Dec;180(23):6298-305. PMID:9829940
  2. ↑ Commichau FM, Wacker I, Schleider J, Blencke HM, Reif I, Tripal P, Stulke J. Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis. J Mol Microbiol Biotechnol. 2007;12(1-2):106-13. PMID:17183217 doi:http://dx.doi.org/10.1159/000096465
  3. ↑ Commichau FM, Gunka K, Landmann JJ, Stulke J. Glutamate metabolism in Bacillus subtilis: gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations of the system. J Bacteriol. 2008 May;190(10):3557-64. doi: 10.1128/JB.00099-08. Epub 2008 Mar 7. PMID:18326565 doi:http://dx.doi.org/10.1128/JB.00099-08

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