3lf0 | pdb_00003lf0

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Template:STRUCTURE 3lf0

Crystal structure of the ATP bound Mycobacterium tuberculosis nitrogen regulatory PII protein

Template:ABSTRACT PUBMED 20521335

Function

[GLNB_MYCTU] In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).

About this Structure

3lf0 is a 3 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

  1. Shetty ND, Reddy MC, Palaninathan SK, Owen JL, Sacchettini JC. Crystal structures of the apo and ATP bound Mycobacterium tuberculosis nitrogen regulatory PII protein. Protein Sci. 2010 Aug;19(8):1513-24. PMID:20521335 doi:10.1002/pro.430

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