|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of a bacterial arylsulfate sulfotransferase catalytic intermediate with 4-nitrophenol bound in the active site== | | ==Crystal structure of a bacterial arylsulfate sulfotransferase catalytic intermediate with 4-nitrophenol bound in the active site== |
| - | <StructureSection load='3ett' size='340' side='right' caption='[[3ett]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3ett' size='340' side='right'caption='[[3ett]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ett]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecol6 Ecol6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ETT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ETT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ett]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_CFT073 Escherichia coli CFT073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ETT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ETT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NPO:P-NITROPHENOL'>NPO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HS8:3-(1-SULFO-1H-IMIDAZOL-3-IUM-4-YL)-L-ALANINE'>HS8</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HS8:3-(1-SULFO-1H-IMIDAZOL-3-IUM-4-YL)-L-ALANINE'>HS8</scene>, <scene name='pdbligand=NPO:P-NITROPHENOL'>NPO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3elq|3elq]], [[3ets|3ets]]</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=3ett FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ett OCA], [https://pdbe.org/3ett PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ett RCSB], [https://www.ebi.ac.uk/pdbsum/3ett PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ett ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASTA, EcF11_2091 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=199310 ECOL6])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aryl-sulfate_sulfotransferase Aryl-sulfate sulfotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.22 2.8.2.22] </span></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=3ett FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ett OCA], [http://pdbe.org/3ett PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ett RCSB], [http://www.ebi.ac.uk/pdbsum/3ett PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ett ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/B3HTA9_ECOLX B3HTA9_ECOLX]] Catalyzes the transfer of sulfuryl groups between phenolic compounds (By similarity).[HAMAP-Rule:MF_00933] | + | [https://www.uniprot.org/uniprot/ASST_ECOL6 ASST_ECOL6] Catalyzes the transfer of sulfuryl groups between phenolic compounds.[HAMAP-Rule:MF_00933]<ref>PMID:18565543</ref> <ref>PMID:19036922</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 21: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Sulfotransferase|Sulfotransferase]] | + | *[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aryl-sulfate sulfotransferase]] | + | [[Category: Escherichia coli CFT073]] |
| - | [[Category: Ecol6]] | + | [[Category: Large Structures]] |
| - | [[Category: Glockshuber, R]] | + | [[Category: Glockshuber R]] |
| - | [[Category: Grimshaw, J P]] | + | [[Category: Grimshaw JP]] |
| - | [[Category: Malojcic, G]] | + | [[Category: Malojcic G]] |
| - | [[Category: Owen, R L]] | + | [[Category: Owen RL]] |
| - | [[Category: Bacteria]]
| + | |
| - | [[Category: Beta propeller]]
| + | |
| - | [[Category: P-nitrophenol]]
| + | |
| - | [[Category: P-nitrophenylsulfate]]
| + | |
| - | [[Category: Phenol]]
| + | |
| - | [[Category: Protein-substrate complex]]
| + | |
| - | [[Category: Sulfate]]
| + | |
| - | [[Category: Sulfohistidine]]
| + | |
| - | [[Category: Transesterification]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase 4-nitrophenol]]
| + | |
| Structural highlights
Function
ASST_ECOL6 Catalyzes the transfer of sulfuryl groups between phenolic compounds.[HAMAP-Rule:MF_00933][1] [2]
Publication Abstract from PubMed
Sulfotransferases are a versatile class of enzymes involved in numerous physiological processes. In mammals, adenosine 3'-phosphate-5'-phosphosulfate (PAPS) is the universal sulfuryl donor, and PAPS-dependent sulfurylation of small molecules, including hormones, sugars, and antibiotics, is a critical step in hepatic detoxification and extracellular signaling. In contrast, little is known about sulfotransferases in bacteria, which make use of sulfurylated molecules as mediators of cell-cell interactions and host-pathogen interactions. Bacterial arylsulfate sulfotransferases (also termed aryl sulfotransferases), in contrast to PAPS-dependent sulfotransferases, transfer sulfuryl groups exclusively among phenolic compounds in a PAPS-independent manner. Here, we report the crystal structure of the virulence factor arylsulfate sulfotransferase (ASST) from the prototypic, pyelonephritogenic Escherichia coli strain CFT073 at 2.0-A resolution, and 2 catalytic intermediates, at 2.1-A and 2.4-A resolution, with substrates bound in the active site. ASST is one of the largest periplasmic enzymes and its 3D structure differs fundamentally from all other structurally characterized sulfotransferases. Each 63.8-kDa subunit of the ASST homodimer comprises a 6-bladed beta-propeller domain and a C-terminal beta-sandwich domain. The active sites of the dimer are situated at the center of the channel formed by each beta-propeller and are defined by the side chains of His-252, His-356, Arg-374, and His-436. We show that ASST follows a ping-pong bi-bi reaction mechanism, in which the catalytic residue His-436 undergoes transient sulfurylation, a previously unreported covalent protein modification. The data provide a framework for understanding PAPS-independent sulfotransfer and a basis for drug design targeting this bacterial virulence factor.
A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sulfotransferase from uropathogenic Escherichia coli.,Malojcic G, Owen RL, Grimshaw JP, Brozzo MS, Dreher-Teo H, Glockshuber R Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19217-22. Epub 2008 Nov 26. PMID:19036922[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Grimshaw JP, Stirnimann CU, Brozzo MS, Malojcic G, Grutter MG, Capitani G, Glockshuber R. DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli. J Mol Biol. 2008 Jul 18;380(4):667-80. Epub 2008 May 20. PMID:18565543 doi:10.1016/j.jmb.2008.05.031
- ↑ Malojcic G, Owen RL, Grimshaw JP, Brozzo MS, Dreher-Teo H, Glockshuber R. A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sulfotransferase from uropathogenic Escherichia coli. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19217-22. Epub 2008 Nov 26. PMID:19036922
- ↑ Malojcic G, Owen RL, Grimshaw JP, Brozzo MS, Dreher-Teo H, Glockshuber R. A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sulfotransferase from uropathogenic Escherichia coli. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19217-22. Epub 2008 Nov 26. PMID:19036922
|
