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Literature summary extracted from

  • Palanca, C.; Rubio, V.
    Effects of T-loop modification on the PII-signalling protein structure of uridylylated Escherichia coli GlnB bound to ATP (2017), Environ. Microbiol. Rep., 9, 290-299 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.59 gene glnD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.59 additional information recombinant production and purification of the uridylylating enzyme GlnD and its use for full uridylylation of large amounts of recombinantly produced pure EcGlnB Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.59 diphosphate + uridylyl-[protein-PII] Escherichia coli
-
 UTP + [protein-PII]
-
 r
2.7.7.59 UTP + [protein-PII] Escherichia coli
-
 diphosphate + uridylyl-[protein-PII]
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.59 Escherichia coli P27249
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.59 recombinant His-tagged enzyme GlnD from Escherichia coli strain BL21(DE3) Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.59 diphosphate + uridylyl-[protein-PII GlnB] substrate GlnK-UMP3, the enzyme acts on residue Tyr51 of GlnB Escherichia coli UTP + [protein-PII GlnK]
-
 r
2.7.7.59 diphosphate + uridylyl-[protein-PII]
-
 Escherichia coli UTP + [protein-PII]
-
 r
2.7.7.59 additional information the bifunctional enzyme GlnD catalyzes the uridylylation and, in the presence of glutamine, the deuridylylation of EcGlnB PII protein Escherichia coli ?
-
-
2.7.7.59 UTP + [protein-PII GlnB] the enzyme acts on residue Tyr51 of GlnK Escherichia coli diphosphate + uridylyl-[protein-PII GlnB]
-
 r
2.7.7.59 UTP + [protein-PII]
-
 Escherichia coli diphosphate + uridylyl-[protein-PII]
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.7.7.59 GlnD
-
 Escherichia coli
2.7.7.59 uridylylating enzyme
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.7.59 metabolism to adapt to environments with variable nitrogen sources and richness, the widely distributed homotrimeric PII signalling proteins bind their allosteric effectors ADP/ATP/2-oxoglutarate, and experience nitrogen-sensitive uridylylation of their flexible T-loops at Tyr51 by enzyme GlnD, regulating their interactions with effector proteins Escherichia coli
2.7.7.59 additional information crystal structure determination and analysis at 1.9 A resolution of the purified Escherichia coli GlnB (EcGlnB) PII protein in fully uridylylated form (EcGlnB-UMP3), structure-function analysis, overview. The T-loop is not visible. Unlike crystalline non-uridylylated EcGlnB, in which T-loops are fixed, uridylylation renders the T-loop highly mobile because of loss of contacts mediated by Tyr51, with concomitant abolition of T-loop anchoring via Arg38 on the ATP site. Analysis of mechanisms of PII selectivity for ATP and of PII-UMP3 signalling, proposing a model for the architecture of the complex of EcGlnBUMP3 with the uridylylation-sensitive PII target ATase (which adenylylates/deadenylylates glutamine synthetase [GS]) and with GS. Good X-ray diffracting crystals of trigonal shape and good size are obtained with fully uridylylated EcGlnB only when ATP, MgCl2 and 2-oxolutarate are present Escherichia coli