2pii | pdb_00002pii

PII, GLNB PRODUCT

spinqualitylabelsall models 2pii, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pii is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: GLNB ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [GLNB_ECOLI] P-II indirectly controls the transcription of the glutamine synthetase 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. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure of the bacterial signal transduction protein P(II) has been refined to an R factor of 13.2% using 3sigma data between 10 and 1.9 A. The crystals exhibited twinning by merohedry and X-ray intensities were corrected using the method of Fisher & Sweet [Fisher & Sweet (1980). Acta Cryst. A36, 755-760] prior to refinement. Our earlier 2.7 A structure [Cheah, Carr, Suffolk, Vasudevan, Dixon & Ollis (1994). Structure, 2, 981-990] served as a starting model. P(II) is a trimeric molecule, each subunit has a mass of 12.4 kDa and contains 112 amino-acid residues. The refined model includes all 1065 protein atoms per subunit plus 312 water molecules. The high-resolution refinement confirms the correctness of our 2.7 A model, although it leads to a redefinition of the extent of various secondary-structural elements. The monomeric structure of P(II) exhibits an interlocking double betaalphabeta fold. This is a stable fold found in a number of proteins with diverse functions. The association of the protein into a trimer leads to a new structure which we describe in detail. The effects of crystal packing forces are discussed and potential interaction sites with other proteins and effector molecules are identified. X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A.,Carr PD, Cheah E, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):93-104. PMID:15299730 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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