Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica.

Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica. Research Abstract Details 

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Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica. Abstract Text:

Amaresh Das,Zheng-Qing Fu,Wolfram Tempel,Zhi-Jie Liu,Jessie Chang,Lirong Chen,Doowon Lee,Weihong Zhou,Hao Xu,Neil Shaw,John P Rose,Lars G Ljungdahl,Bi-Cheng Wang,

The strict anaerobic, thermophilic bacterium Moorella thermoacetica metabolizes C1 compounds for example CO(2)/H(2), CO, formate, and methanol into acetate via the Wood/Ljungdahl pathway. Some of the key steps in this pathway include the metabolism of the C1 compounds into the methyl group of methylenetetrahydrofolate (MTHF) and the transfer of the methyl group from MTHF to the methyl group of acetyl-CoA catalyzed by methyltransferase, corrinoid protein and CO dehydrogenase/acetyl CoA synthase. Recently, we reported the crystallization of a 25 kDa methanol-induced corrinoid protein from M. thermoacetica (Zhou et al., Acta Crystallogr F 2005; 61:537-540). In this study we analyzed the crystal structure of the 25 kDa protein and provide genetic and biochemical evidences supporting its role in the methanol metabolism of M. thermoacetia. The 25 kDa protein was encoded by orf1948 of contig 303 in the M. thermoacetica genome. It resembles similarity to MtaC the corrinoid protein of the methanol:CoM methyltransferase system of methane producing archaea. The latter enzyme system also contains two additional enzymes MtaA and MtaB. Homologs of MtaA and MtaB were found to be encoded by orf2632 of contig 303 and orf1949 of contig 309, respectively, in the M. thermoacetica genome. The orf1948 and orf1949 were co-transcribed from a single polycistronic operon. Metal analysis and spectroscopic data confirmed the presence of cobalt and the corrinoid in the purified 25 kDa protein. High resolution X-ray crystal structure of the purified 25 kDa protein revealed corrinoid as methylcobalamin with the imidazole of histidine as the alpha-axial ligand replacing benziimidazole, suggesting base-off configuration for the corrinoid. Methanol significantly activated the expression of the 25 kDa protein. Cyanide and nitrate inhibited methanol metabolism and suppressed the level of the 25 kDa protein. The results suggest a role of the 25 kDa protein in the methanol metabolism of M. thermoacetica.

Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica. Publishing Authors By Initials

A Das,ZQ Fu,W Tempel,ZJ Liu,J Chang,L Chen,D Lee,W Zhou,H Xu,N Shaw,JP Rose,LG Ljungdahl,BC Wang,

For similar investigative techniques: genetic techniques: sequence alignment research abstracts see: investigative techniques: genetic techniques: sequence alignment research

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Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Proteins

VOLUME: 67

Page Numbers: 167-76

Journal Abbreviation: Proteins

ISSN: 1097-0134

DAY: 1

MONTH: Apr

YEAR: 2007

Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8700181

Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica. Keywords Mesh Terms:

KEYWORDS: Sequence Alignment

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica. Information

Substance Name: Methanol

Registry Number: 67-56-1

Grant and Affiliation Information for Characterization of a corrinoid protein involved in the C1 metabolism of strict anaerobic bacterium Moorella thermoacetica.

AFFILIATION: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: 1P50 GM62407

ACRONYM: GM

MEDLINETA: Proteins

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