Crystal structure of Aquifex aeolicus gene product Aq1627: a putative phosphoglucosamine mutase reveals a unique C-terminal end-to-end disulfide linkage

The crystal structure of Aq1627 protein from Aquifex aeolicus, a hyperthermophilic bacterium has been solved, which reveals a unique end-to-end disulfide linkage.

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Faculty Opinions recommendation of The crystal structure of the Escherichia coli YfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1014428.193478 ◽

2003 ◽

Author(s):

Wolfgang Buckel

Keyword(s):

Crystal Structure ◽

Escherichia Coli ◽

Gene Product ◽

Wide Family

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A new sulfurtransferase from the hyperthermophilic bacterium Aquifex aeolicus

FEBS Journal ◽

10.1111/j.1742-4658.2007.05985.x ◽

2007 ◽

Vol 274 (17) ◽

pp. 4572-4587 ◽

Cited By ~ 17

Author(s):

Marie-Cécile Giuliani ◽

Pascale Tron ◽

Gisèle Leroy ◽

Corinne Aubert ◽

Patrick Tauc ◽

...

Keyword(s):

Aquifex Aeolicus ◽

Hyperthermophilic Bacterium

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Crystal structure and magnetic properties of [Cu2(tmen)2(N3)3](PF6) (tmen = N,N,N',N'-tetramethylethylenediamine): a copper(II) chain compound with both single symmetrical and double dissymmetrical end-to-end azido bridges

Inorganic Chemistry ◽

10.1021/ic00194a011 ◽

1984 ◽

Vol 23 (26) ◽

pp. 4454-4459 ◽

Cited By ~ 41

Author(s):

Itka Bkouche-Waksman ◽

Marie Laure Boillot ◽

Olivier Kahn ◽

Sonia Sikorav

Keyword(s):

Crystal Structure ◽

Magnetic Properties ◽

End To End ◽

Chain Compound

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ChemInform Abstract: CRYSTAL STRUCTURE AND MAGNETIC PROPERTIES OF (CU2(TMEN)2(N3)3)(PF6) (TMEN = N,N,N′,N′-TETRAMETHYLETHYLENEDIAMINE): A COPPER(II) CHAIN COMPOUND WITH BOTH SINGLE SYMMETRICAL AND DOUBLE DISSYMMETRICAL END-TO-END AZIDO BRIDGES

Chemischer Informationsdienst ◽

10.1002/chin.198520075 ◽

1985 ◽

Vol 16 (20) ◽

Author(s):

I. BKOUCHE-WAKSMAN ◽

M.-L. BOILLOT ◽

O. KAHN ◽

S. SIKORAV

Keyword(s):

Crystal Structure ◽

Magnetic Properties ◽

End To End ◽

Chain Compound

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Minimal and RNA-free RNase P in Aquifex aeolicus

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1707862114 ◽

2017 ◽

Vol 114 (42) ◽

pp. 11121-11126 ◽

Cited By ~ 19

Author(s):

Astrid I. Nickel ◽

Nadine B. Wäber ◽

Markus Gößringer ◽

Marcus Lechner ◽

Uwe Linne ◽

...

Keyword(s):

Escherichia Coli ◽

Saccharomyces Cerevisiae ◽

Gene Transfer ◽

Horizontal Gene Transfer ◽

Rnase P ◽

Aquifex Aeolicus ◽

Trna Processing ◽

Hyperthermophilic Bacterium ◽

Domains Of Life

RNase P is an essential tRNA-processing enzyme in all domains of life. We identified an unknown type of protein-only RNase P in the hyperthermophilic bacterium Aquifex aeolicus: Without an RNA subunit and the smallest of its kind, the 23-kDa polypeptide comprises a metallonuclease domain only. The protein has RNase P activity in vitro and rescued the growth of Escherichia coli and Saccharomyces cerevisiae strains with inactivations of their more complex and larger endogenous ribonucleoprotein RNase P. Homologs of Aquifex RNase P (HARP) were identified in many Archaea and some Bacteria, of which all Archaea and most Bacteria also encode an RNA-based RNase P; activity of both RNase P forms from the same bacterium or archaeon could be verified in two selected cases. Bioinformatic analyses suggest that A. aeolicus and related Aquificaceae likely acquired HARP by horizontal gene transfer from an archaeon.

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