1v47

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{{STRUCTURE_1v47| PDB=1v47 | SCENE= }}
{{STRUCTURE_1v47| PDB=1v47 | SCENE= }}
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'''Crystal structure of ATP sulfurylase from Thermus thermophillus HB8 in complex with APS'''
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===Crystal structure of ATP sulfurylase from Thermus thermophillus HB8 in complex with APS===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15065853}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15065853 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15065853}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of a novel zinc-binding ATP sulfurylase from Thermus thermophilus HB8., Taguchi Y, Sugishima M, Fukuyama K, Biochemistry. 2004 Apr 13;43(14):4111-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15065853 15065853]
Crystal structure of a novel zinc-binding ATP sulfurylase from Thermus thermophilus HB8., Taguchi Y, Sugishima M, Fukuyama K, Biochemistry. 2004 Apr 13;43(14):4111-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15065853 15065853]
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Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8., Taguchi Y, Hoseki J, Kakuta Y, Fukuyama K, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1645-7. Epub 2003, Aug 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12925800 12925800]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sulfate adenylyltransferase]]
[[Category: Sulfate adenylyltransferase]]
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Zinc]]
[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:03:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:00:16 2008''

Revision as of 07:00, 29 July 2008

Image:1v47.png

Template:STRUCTURE 1v47

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

Template:ABSTRACT PUBMED 15065853

About this Structure

1V47 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a novel zinc-binding ATP sulfurylase from Thermus thermophilus HB8., Taguchi Y, Sugishima M, Fukuyama K, Biochemistry. 2004 Apr 13;43(14):4111-8. PMID:15065853

Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8., Taguchi Y, Hoseki J, Kakuta Y, Fukuyama K, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1645-7. Epub 2003, Aug 19. PMID:12925800

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