1V47

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

Summary for 1V47

• Entry DOI: 10.2210/pdb1v47/pdb
• Descriptor: ATP sulfurylase, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: product binding complex, zinc, riken structural genomics/proteomics initiative, rsgi, structural genomics, transferase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 79050.65

Authors

Taguchi, Y.,Sugishima, M.,Fukuyama, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-11-11, release date: 2004-04-06, Last modification date: 2023-10-25)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.49 Å)