1V47

Crystal structure of ATP sulfurylase from Thermus thermophillus HB8 in complex with APS

1V47 の概要

• エントリーDOI: 10.2210/pdb1v47/pdb
• 分子名称: ATP sulfurylase, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: product binding complex, zinc, riken structural genomics/proteomics initiative, rsgi, structural genomics, transferase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79050.65

構造登録者

Taguchi, Y.,Sugishima, M.,Fukuyama, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-11-11, 公開日: 2004-04-06, 最終更新日: 2023-10-25)

主引用文献

Taguchi, Y.,Sugishima, M.,Fukuyama, K.
Crystal structure of a novel zinc-binding ATP sulfurylase from Thermus thermophilus HB8
Biochemistry, 43:4111-4118, 2004

PubMed Abstract: ATP sulfurylase (ATPS) is a ubiquitous enzyme that catalyzes the transfer of the adenylyl group from ATP to inorganic sulfate, producing adenosine 5'-phosphosulfate (APS) and pyrophosphate. The crystal structure of ATPS from Thermus thermophilus HB8 (TtATPS, 347 amino acid residues) in complex with APS was determined at 2.5 A resolution. TtATPS is composed of three domains [domain I (residues 1-134), domain II (residues 135-290), and domain III (residues 291-347)], like the Riftia pachyptila symbiont ATPS, but lacks a fourth domain present in ATPSs from the yeast Saccharomyces cerevisiae and from the fungus Penicillium chrysogenum. TtATPS forms a dimer in the crystal, and the manner of subunit association is different from that observed in dimeric R. pachyptila symbiont ATPS and in the hexameric S. cerevisiae and P. chrysogenum ATPSs. APS is located in the active site of TtATPS, which contains several motifs (QXRN, HXXH, and GRD) conserved in ATPSs. Unexpectedly, TtATPS binds one metal ion per subunit in domain III. XAFS measurement of the crystal and the Bijvoet difference Fourier map unambiguously characterized the metal ion as a zinc ion. The zinc ion is tetrahedrally coordinated by Cys294, Cys297, Cys306, and His310, and could not be removed from the protein by treatment with EDTA. The zinc ion binding site is far from the active site. Because all four residues coordinated to the zinc ion are conserved in the ATPSs from thermophilic bacteria such as Archaeoglobus fulgidus, Pyrococcus abyssi, and Sulfolobus solfataricus, zinc ion chelation may contribute to the thermal stability of these ATPSs.

PubMed: 15065853
DOI: 10.1021/bi036052t

実験手法

X-RAY DIFFRACTION (2.49 Å)