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| ==Crystal structure of ATP sulfurylase from Thermus thermophillus HB8 in complex with APS== | | ==Crystal structure of ATP sulfurylase from Thermus thermophillus HB8 in complex with APS== |
- | <StructureSection load='1v47' size='340' side='right' caption='[[1v47]], [[Resolution|resolution]] 2.49Å' scene=''> | + | <StructureSection load='1v47' size='340' side='right'caption='[[1v47]], [[Resolution|resolution]] 2.49Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1v47]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V47 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v47]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V47 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49Å</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v47 OCA], [http://pdbe.org/1v47 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v47 RCSB], [http://www.ebi.ac.uk/pdbsum/1v47 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v47 ProSAT], [http://www.topsan.org/Proteins/RSGI/1v47 TOPSAN]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v47 OCA], [https://pdbe.org/1v47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v47 RCSB], [https://www.ebi.ac.uk/pdbsum/1v47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v47 ProSAT], [https://www.topsan.org/Proteins/RSGI/1v47 TOPSAN]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q5SKH7_THET8 Q5SKH7_THET8] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | + | [[Category: Large Structures]] |
- | [[Category: Sulfate adenylyltransferase]] | + | [[Category: Thermus thermophilus]] |
- | [[Category: Fukuyama, K]] | + | [[Category: Fukuyama K]] |
- | [[Category: Structural genomic]]
| + | [[Category: Sugishima M]] |
- | [[Category: Sugishima, M]] | + | [[Category: Taguchi Y]] |
- | [[Category: Taguchi, Y]] | + | |
- | [[Category: Product binding complex]]
| + | |
- | [[Category: Rsgi]]
| + | |
- | [[Category: Transferase]]
| + | |
- | [[Category: Zinc]]
| + | |
| Structural highlights
1v47 is a 2 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Method: | X-ray diffraction, Resolution 2.49Å |
Ligands: | , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN |
Function
Q5SKH7_THET8
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Taguchi Y, Sugishima M, Fukuyama K. Crystal structure of a novel zinc-binding ATP sulfurylase from Thermus thermophilus HB8. Biochemistry. 2004 Apr 13;43(14):4111-8. PMID:15065853 doi:10.1021/bi036052t
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