D
IPR022667

Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, N-terminal

InterPro entry
Short nameForMFR_H4MPT_ForTrfase_N
Overlapping
homologous
superfamilies
 

Description

Formylmethanofuran:tetrahyromethanopterin formyltransferase (Ftr) is involved in C1 metabolism in methanogenic archaea, sulphate-reducing archaea and methylotrophic bacteria. It catalyses the following reversible reaction:

N-formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin

Ftr from the thermophilic methanogen Methanopyrus kandleri (optimum growth temperature 98 degrees C) is a hyperthermophilic enzyme that is absolutely dependent on the presence of lyotropic salts for activity and thermostability. The crystal structure of Ftr, determined to a reveals a homotetramer composed essentially of two dimers. Each subunit is subdivided into two tightly associated lobes both consisting of a predominantly antiparallel β sheet flanked by α helices forming an α/β sandwich structure. The approximate location of the active site was detected in a region close to the dimer interface
[3]
. Ftr from the mesophilic methanogen Methanosarcina barkeri and the sulphate-reducing archaeon Archaeoglobus fulgidus have a similar structure
[2]
.

In the methylotrophic bacterium Methylobacterium extorquens, Ftr interacts with three other polypeptides to form an Ftr/cyclohydrolase complex which catalyses the hydrolysis of formyl-tetrahydromethanopterin to formate during growth on C1 substrates
[1]
.

This entry represents the ferredoxin-like Ftr N-terminal domain.

References

1.Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1. Pomper BK, Saurel O, Milon A, Vorholt JA. FEBS Lett. 523, 133-7, (2002). View articlePMID: 12123819

2.Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship. Mamat B, Roth A, Grimm C, Ermler U, Tziatzios C, Schubert D, Thauer RK, Shima S. Protein Sci. 11, 2168-78, (2002). View articlePMID: 12192072

3.Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability. Ermler U, Merckel M, Thauer R, Shima S. Structure 5, 635-46, (1997). View articlePMID: 9195883

GO terms

cellular component

  • None

Cross References

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