1v47
From Proteopedia
(New page: 200px<br /><applet load="1v47" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v47, resolution 2.49Å" /> '''Crystal structure of...) |
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| - | [[Image:1v47.gif|left|200px]]<br /><applet load="1v47" size=" | + | [[Image:1v47.gif|left|200px]]<br /><applet load="1v47" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1v47, resolution 2.49Å" /> | caption="1v47, resolution 2.49Å" /> | ||
'''Crystal structure of ATP sulfurylase from Thermus thermophillus HB8 in complex with APS'''<br /> | '''Crystal structure of ATP sulfurylase from Thermus thermophillus HB8 in complex with APS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ATP sulfurylase (ATPS) is a ubiquitous enzyme that catalyzes the transfer | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1V47 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with ZN, CL, NA and ADX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] Full crystallographic information is available from [http:// | + | 1V47 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=ADX:'>ADX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V47 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Fukuyama, K.]] | [[Category: Fukuyama, K.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sugishima, M.]] | [[Category: Sugishima, M.]] | ||
[[Category: Taguchi, Y.]] | [[Category: Taguchi, Y.]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:31:17 2008'' |
Revision as of 13:31, 21 February 2008
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Crystal structure of ATP sulfurylase from Thermus thermophillus HB8 in complex with APS
Overview
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.
About this Structure
1V47 is a Single protein structure of sequence from Thermus thermophilus with , , and as ligands. Active as Sulfate adenylyltransferase, with EC number 2.7.7.4 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
Page seeded by OCA on Thu Feb 21 15:31:17 2008
Categories: Single protein | Sulfate adenylyltransferase | Thermus thermophilus | Fukuyama, K. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sugishima, M. | Taguchi, Y. | ADX | CL | NA | ZN | Product binding complex | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics | Zinc
