6IOW
Crystal structure of Porphyromonas gingivalis phosphotransacetylase
Summary for 6IOW
| Entry DOI | 10.2210/pdb6iow/pdb |
| Descriptor | Phosphotransacetylase (2 entities in total) |
| Functional Keywords | porphyromonas gingivalis, phosphotransacetylase, atp, essential gene, transferase |
| Biological source | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
| Total number of polymer chains | 2 |
| Total formula weight | 72295.47 |
| Authors | Kezuka, Y.,Yoshida, Y.,Nonaka, T. (deposition date: 2018-10-31, release date: 2019-04-24, Last modification date: 2023-11-22) |
| Primary citation | Yoshida, Y.,Sato, M.,Nonaka, T.,Hasegawa, Y.,Kezuka, Y. Characterization of the phosphotransacetylase-acetate kinase pathway for ATP production inPorphyromonas gingivalis. J Oral Microbiol, 11:1588086-1588086, 2019 Cited by PubMed Abstract: Acetyl phosphate (AcP) is generally produced from acetyl coenzyme A by phosphotransacetylase (Pta), and subsequent reaction with ADP, catalyzed by acetate kinase (Ack), produces ATP. The mechanism of ATP production in is poorly understood. The aim of this study was to explore the molecular basis of the Pta-Ack pathway in this microorganism. Pta and Ack from ATCC 33277 were enzymatically and structurally characterized. Structural and mutational analyses suggest that Pta is a dimer with two substrate-binding sites in each subunit. Ack is also dimeric, with a catalytic cleft in each subunit, and structural analysis indicates a dramatic domain motion that opens and closes the cleft during catalysis. ATP formation by Ack proceeds via a sequential mechanism. Reverse transcription-PCR analysis demonstrated that the () and () genes, tandemly located in the genome, are cotranscribed as an operon. Inactivation of or in by homologous recombination was successful only when the inactivated gene was expressed . Therefore, both and genes are essential for this microorganism. Insights into the Pta-Ack pathway reported herein would be helpful to understand the energy acquisition in . PubMed: 31007866DOI: 10.1080/20002297.2019.1588086 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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