Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon

被引:74
|
作者
Smeulders, Marjan J. [1 ]
Barends, Thomas R. M. [2 ]
Pol, Arjan [1 ]
Scherer, Anna [2 ]
Zandvoort, Marcel H. [1 ]
Udvarhelyi, Aniko [2 ]
Khadem, Ahmad F. [1 ]
Menzel, Andreas [3 ]
Hermans, John [1 ]
Shoeman, Robert L. [2 ]
Wessels, Hans J. C. T. [4 ]
van den Heuvel, Lambert P. [4 ]
Russ, Lina [1 ]
Schlichting, Ilme [2 ]
Jetten, Mike S. M. [1 ]
den Camp, Huub J. M. Op [1 ]
机构
[1] Radboud Univ Nijmegen, Dept Microbiol, NL-6525 AJ Nijmegen, Netherlands
[2] Max Planck Inst Med Res, Dept Biomol Mech, D-69120 Heidelberg, Germany
[3] Paul Scherrer Inst, CH-5232 Villigen, Switzerland
[4] Radboud Univ Nijmegen, Nijmegen Ctr Mitochondrial Disorders, Nijmegen Prote Facil, Dept Lab Med,Med Ctr, NL-6500 HB Nijmegen, Netherlands
关键词
SULFUR-COMPOUNDS; SULFIDE COS; ANHYDRASE; SUBSTRATE; MODEL; CS2; MACROMOLECULES; CONSUMPTION; METABOLISM; SCATTERING;
D O I
10.1038/nature10464
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Extremophilic organisms require specialized enzymes for their exotic metabolisms. Acid-loving thermophilic Archaea that live in the mudpots of volcanic solfataras obtain their energy from reduced sulphur compounds such as hydrogen sulphide (H2S) and carbon disulphide (CS2)(1,2). The oxidation of these compounds into sulphuric acid creates the extremely acidic environment that characterizes solfataras. The hyperthermophilic Acidianus strain A1-3, which was isolated from the fumarolic, ancient sauna building at the Solfatara volcano (Naples, Italy), was shown to rapidly convert CS2 into H2S and carbon dioxide (CO2), but nothing has been known about the modes of action and the evolution of the enzyme(s) involved. Here we describe the structure, the proposed mechanism and evolution of a CS2 hydrolase from Acidianus A1-3. The enzyme monomer displays a typical beta-carbonic anhydrase fold and active site, yet CO2 is not one of its substrates. Owing to large carboxy-and amino-terminal arms, an unusual hexadecameric catenane oligomer has evolved. This structure results in the blocking of the entrance to the active site that is found in canonical beta-carbonic anhydrases and the formation of a single 15-angstrom-long, highly hydrophobic tunnel that functions as a specificity filter. The tunnel determines the enzyme's substrate specificity for CS2, which is hydrophobic. The transposon sequences that surround the gene encoding this CS2 hydrolase point to horizontal gene transfer as a mechanism for its acquisition during evolution. Our results show how the ancient beta-carbonic anhydrase, which is central to global carbon metabolism, was transformed by divergent evolution into a crucial enzyme in CS2 metabolism.
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收藏
页码:412 / +
页数:8
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