1JHD

Crystal Structure of Bacterial ATP Sulfurylase from the Riftia pachyptila Symbiont

1JHD の概要

• エントリーDOI: 10.2210/pdb1jhd/pdb
• 分子名称: SULFATE ADENYLYLTRANSFERASE, SULFATE ION, BROMIDE ION, ... (4 entities in total)
• 機能のキーワード: adenylyl transferase, sulfurylase, aps, chemoautotroph, bromide, transferase
• 由来する生物種: Sulfur-oxidizing endosymbiont of Riftia pachyptila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44869.42

構造登録者

Beynon, J.D.,MacRae, I.J.,Huston, S.L.,Nelson, D.C.,Segel, I.H.,Fisher, A.J. (登録日: 2001-06-27, 公開日: 2001-12-07, 最終更新日: 2024-02-07)

主引用文献

Beynon, J.D.,MacRae, I.J.,Huston, S.L.,Nelson, D.C.,Segel, I.H.,Fisher, A.J.
Crystal structure of ATP sulfurylase from the bacterial symbiont of the hydrothermal vent tubeworm Riftia pachyptila.
Biochemistry, 40:14509-14517, 2001

PubMed Abstract: In sulfur chemolithotrophic bacteria, the enzyme ATP sulfurylase functions to produce ATP and inorganic sulfate from APS and inorganic pyrophosphate, which is the final step in the biological oxidation of hydrogen sulfide to sulfate. The giant tubeworm, Riftia pachyptila, which lives near hydrothermal vents on the ocean floor, harbors a sulfur chemolithotroph as an endosymbiont in its trophosome tissue. This yet-to-be-named bacterium was found to contain high levels of ATP sulfurylase that may provide a substantial fraction of the organisms ATP. We present here, the crystal structure of ATP sulfurylase from this bacterium at 1.7 A resolution. As predicted from sequence homology, the enzyme folds into distinct N-terminal and catalytic domains, but lacks the APS kinase-like C-terminal domain that is present in fungal ATP sulfurylase. The enzyme crystallizes as a dimer with one subunit in the crystallographic asymmetric unit. Many buried solvent molecules mediate subunit contacts at the interface. Despite the high concentration of sulfate needed for crystallization, no ordered sulfate was observed in the sulfate-binding pocket. The structure reveals a mobile loop positioned over the active site. This loop is in a "closed" or "down" position in the reported crystal structures of fungal ATP sulfurylases, which contained bound substrates, but it is in an "open" or "up" position in the ligand-free Riftia symbiont enzyme. Thus, closure of the loop correlates with occupancy of the active site, although the loop itself does not interact directly with bound ligands. Rather, it appears to assist in the orientation of residues that do interact with active-site ligands. Amino acid differences between the mobile loops of the enzymes from sulfate assimilators and sulfur chemolithotrophs may account for the significant kinetic differences between the two classes of ATP sulfurylase.

PubMed: 11724564
DOI: 10.1021/bi015643l

実験手法

X-RAY DIFFRACTION (1.7 Å)