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Zinc plays a key role in human and bacterial GTP cyclohydrolase I.

Auerbach G, Herrmann A, Bracher A, Bader G, Gutlich M, Fischer M, Neukamm M, Garrido-Franco M, Richardson J, Nar H, Huber R, Bacher A
Proc Natl Acad Sci U S A 97 13567-72 (2000)
Cited: 69 times
EuropePMC logo PMID: 11087827

Abstract

The crystal structure of recombinant human GTP cyclohydrolase I was solved by Patterson search methods by using the coordinates of the Escherichia coli enzyme as a model. The human as well as bacterial enzyme were shown to contain an essential zinc ion coordinated to a His side chain and two thiol groups in each active site of the homodecameric enzymes that had escaped detection during earlier studies of the E. coli enzyme. The zinc ion is proposed to generate a hydroxyl nucleophile for attack of imidazole ring carbon atom eight of the substrate, GTP. It may also be involved in the hydrolytic release of formate from the intermediate, 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate, and in the consecutive Amadori rearrangement of the ribosyl moiety.

Articles - 1fbx mentioned but not cited (5)

  1. Zinc plays a key role in human and bacterial GTP cyclohydrolase I. Auerbach G, Herrmann A, Bracher A, Bader G, Gutlich M, Fischer M, Neukamm M, Garrido-Franco M, Richardson J, Nar H, Huber R, Bacher A. Proc Natl Acad Sci U S A 97 13567-13572 (2000)
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  4. Crystallization and preliminary X-ray characterization of the nitrile reductase QueF: a queuosine-biosynthesis enzyme. Swairjo MA, Reddy RR, Lee B, Van Lanen SG, Brown S, de Crécy-Lagard V, Iwata-Reuyl D, Schimmel P. Acta Crystallogr Sect F Struct Biol Cryst Commun 61 945-948 (2005)
  5. GTP cyclohydrolase I activity from Rickettsia monacensis strain Humboldt, a rickettsial endosymbiont of Ixodes pacificus. Bodnar J, Fitch S, Sanchez J, Lesser M, Baston DS, Zhong J. Ticks Tick Borne Dis 11 101434 (2020)


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