4p07: Difference between revisions
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==Bacterial aryl sulfotransferase (ASST) soaked with human urine== | |||
<StructureSection load='4p07' size='340' side='right'caption='[[4p07]], [[Resolution|resolution]] 2.59Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4p07]] 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=4P07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P07 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4p07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p07 OCA], [https://pdbe.org/4p07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p07 RCSB], [https://www.ebi.ac.uk/pdbsum/4p07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p07 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0D6H805_ECOLX A0A0D6H805_ECOLX] Catalyses the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds.[HAMAP-Rule:MF_00933] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial aryl sulfotransferases (ASSTs) catalyze sulfotransfer from a phenolic sulfate to a phenol. These enzymes are frequently found in pathogens and upregulated during infection. Their mechanistic understanding is very limited, and their natural substrates are unknown. Here, the crystal structures of Escherichia coli CFT073 ASST trapped in its presulfurylation state with model donor substrates bound in the active site are reported, which reveal the molecular interactions governing substrate recognition. Furthermore, spectroscopic titrations with donor substrates and sulfurylation kinetics of ASST illustrate that this enzyme binds substrates in a 1:1 stoichiometry and that the active sites of the ASST homooligomer act independently. Mass spectrometry and crystallographic experiments of ASST incubated with human urine demonstrate that urine contains a sulfuryl donor substrate. In addition, we examined the capability of the two paralogous dithiol oxidases present in uropathogenic E. coli CFT073, DsbA, and the ASST-specific enzyme DsbL, to introduce the single, conserved disulfide bond into ASST. We show that DsbA and DsbL introduce the disulfide bond into unfolded ASST at similar rates. Hence, a chaperone effect of DsbL, not present in DsbA, appears to be responsible for the dependence of efficient ASST folding on DsbL in vivo. The conservation of paralogous dithiol oxidases with different substrate specificities in certain bacterial strains may therefore be a consequence of the complex folding pathways of their substrate proteins. | |||
Structural and Mechanistic Insights into the PAPS-Independent Sulfotransfer Catalyzed by Bacterial Aryl Sulfotransferase and the Role of the DsbL/DsbI System in Its Folding.,Malojcic G, Owen RL, Glockshuber R Biochemistry. 2014 Mar 25;53(11):1870-7. doi: 10.1021/bi401725j. Epub 2014 Mar, 13. PMID:24601529<ref>PMID:24601529</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4p07" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli CFT073]] | |||
[[Category: Large Structures]] | |||
[[Category: Glockshuber R]] | |||
[[Category: Malojcic G]] | |||
[[Category: Owen RL]] | |||
Latest revision as of 11:25, 23 October 2024
Bacterial aryl sulfotransferase (ASST) soaked with human urineBacterial aryl sulfotransferase (ASST) soaked with human urine
Structural highlights
FunctionA0A0D6H805_ECOLX Catalyses the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds.[HAMAP-Rule:MF_00933] Publication Abstract from PubMedBacterial aryl sulfotransferases (ASSTs) catalyze sulfotransfer from a phenolic sulfate to a phenol. These enzymes are frequently found in pathogens and upregulated during infection. Their mechanistic understanding is very limited, and their natural substrates are unknown. Here, the crystal structures of Escherichia coli CFT073 ASST trapped in its presulfurylation state with model donor substrates bound in the active site are reported, which reveal the molecular interactions governing substrate recognition. Furthermore, spectroscopic titrations with donor substrates and sulfurylation kinetics of ASST illustrate that this enzyme binds substrates in a 1:1 stoichiometry and that the active sites of the ASST homooligomer act independently. Mass spectrometry and crystallographic experiments of ASST incubated with human urine demonstrate that urine contains a sulfuryl donor substrate. In addition, we examined the capability of the two paralogous dithiol oxidases present in uropathogenic E. coli CFT073, DsbA, and the ASST-specific enzyme DsbL, to introduce the single, conserved disulfide bond into ASST. We show that DsbA and DsbL introduce the disulfide bond into unfolded ASST at similar rates. Hence, a chaperone effect of DsbL, not present in DsbA, appears to be responsible for the dependence of efficient ASST folding on DsbL in vivo. The conservation of paralogous dithiol oxidases with different substrate specificities in certain bacterial strains may therefore be a consequence of the complex folding pathways of their substrate proteins. Structural and Mechanistic Insights into the PAPS-Independent Sulfotransfer Catalyzed by Bacterial Aryl Sulfotransferase and the Role of the DsbL/DsbI System in Its Folding.,Malojcic G, Owen RL, Glockshuber R Biochemistry. 2014 Mar 25;53(11):1870-7. doi: 10.1021/bi401725j. Epub 2014 Mar, 13. PMID:24601529[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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