The crystal structure of a novel phosphopantothenate synthetase from the hyperthermophilic archaea, Thermococcus onnurineus NA1

Min Kyu Kim; Young Jun An; Sun Shin Cha

doi:10.1016/j.bbrc.2013.09.008

The crystal structure of a novel phosphopantothenate synthetase from the hyperthermophilic archaea, Thermococcus onnurineus NA1

Min Kyu Kim, Young Jun An, Sun Shin Cha

Chemistry & Nanoscience

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Pantothenate is the essential precursor of coenzyme A (CoA), a fundamental cofactor in all aspects of metabolism. In bacteria and eukaryotes, pantothenate synthetase (PS) catalyzes the last step in the pantothenate biosynthetic pathway, and pantothenate kinase (PanK) phosphorylates pantothenate for its entry into the CoA biosynthetic pathway. However, genes encoding PS and PanK have not been identified in archaeal genomes. Recently, a comparative genomic analysis and the identification and characterization of two novel archaea-specific enzymes show that archaeal pantoate kinase (PoK) and phosphopantothenate synthetase (PPS) represent counterparts to the PS/PanK pathway in bacteria and eukaryotes. The TON1374 protein from Thermococcus onnurineus NA1 is a PPS, that shares 54% sequence identity with the first reported archaeal PPS candidate, MM2281, from Methanosarcina mazei and 91% sequence identity with TK1686, the PPS from Thermococcus kodakarensis. Here, we report the apo and ATP-complex structures of TON1374 and discuss the substrate-binding mode and reaction mechanism.

Original language	English
Pages (from-to)	533-538
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	439
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2013.09.008
State	Published - 4 Oct 2013

Bibliographical note

Funding Information:
We thank the beamline staff at BL-5C, PLS, Republic of Korea and BL-17A, PF, Japan for support with the data collection. This work was supported by the National Research Foundation of Korea Grant ( NRF-2012R1A2A2A02005978 ), the Marine and Extreme Genome Research Center program and the Development of Biohydrogen Production Technology Using Hyperthermophilic Archaea program of MLTM, and the KIOST in-house NSC program.

Keywords

Archaea
Coenzyme A biosynthesis
Crystal structure of TON1374
Crystal structure of TON1374/ATP complex
Phosphopantothenate synthetase

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10.1016/j.bbrc.2013.09.008

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title = "The crystal structure of a novel phosphopantothenate synthetase from the hyperthermophilic archaea, Thermococcus onnurineus NA1",

abstract = "Pantothenate is the essential precursor of coenzyme A (CoA), a fundamental cofactor in all aspects of metabolism. In bacteria and eukaryotes, pantothenate synthetase (PS) catalyzes the last step in the pantothenate biosynthetic pathway, and pantothenate kinase (PanK) phosphorylates pantothenate for its entry into the CoA biosynthetic pathway. However, genes encoding PS and PanK have not been identified in archaeal genomes. Recently, a comparative genomic analysis and the identification and characterization of two novel archaea-specific enzymes show that archaeal pantoate kinase (PoK) and phosphopantothenate synthetase (PPS) represent counterparts to the PS/PanK pathway in bacteria and eukaryotes. The TON1374 protein from Thermococcus onnurineus NA1 is a PPS, that shares 54% sequence identity with the first reported archaeal PPS candidate, MM2281, from Methanosarcina mazei and 91% sequence identity with TK1686, the PPS from Thermococcus kodakarensis. Here, we report the apo and ATP-complex structures of TON1374 and discuss the substrate-binding mode and reaction mechanism.",

keywords = "Archaea, Coenzyme A biosynthesis, Crystal structure of TON1374, Crystal structure of TON1374/ATP complex, Phosphopantothenate synthetase",

author = "Kim, {Min Kyu} and An, {Young Jun} and Cha, {Sun Shin}",

note = "Funding Information: We thank the beamline staff at BL-5C, PLS, Republic of Korea and BL-17A, PF, Japan for support with the data collection. This work was supported by the National Research Foundation of Korea Grant ( NRF-2012R1A2A2A02005978 ), the Marine and Extreme Genome Research Center program and the Development of Biohydrogen Production Technology Using Hyperthermophilic Archaea program of MLTM, and the KIOST in-house NSC program. ",

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The crystal structure of a novel phosphopantothenate synthetase from the hyperthermophilic archaea, Thermococcus onnurineus NA1

Abstract

Bibliographical note

Keywords

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