3elq: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3elq.png|left|200px]]
-<!--
+==Crystal structure of a bacterial arylsulfate sulfotransferase==
-The line below this paragraph, containing "STRUCTURE_3elq", creates the "Structure Box" on the page.
+<StructureSection load='3elq' size='340' side='right'caption='[[3elq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3elq]] 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=3ELQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ELQ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_3elq|  PDB=3elq  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3elq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3elq OCA], [https://pdbe.org/3elq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3elq RCSB], [https://www.ebi.ac.uk/pdbsum/3elq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3elq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ASST_ECOL6 ASST_ECOL6] Catalyzes the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds. In vitro, is able to use 4-methylumbelliferyl sulfate and p-nitrophenyl sulfate (PNS) as donor substrates with phenol as the acceptor substrate (PubMed:18565543, PubMed:19036922). Cannot use 3'-phosphoadenosine-5'-phophosulfate (PAPS), the donor substrate of mammalian sulfotransferase (PubMed:19036922).<ref>PMID:18565543</ref> <ref>PMID:19036922</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/3elq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3elq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===Crystal structure of a bacterial arylsulfate sulfotransferase===
+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<ref>PMID:19036922</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3elq" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19036922}}, adds the Publication Abstract to the page
+*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19036922 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19036922}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia coli CFT073]]
-ELQ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ELQ OCA].
+[[Category: Large Structures]]
+[[Category: Glockshuber R]]
-==Reference==
+[[Category: Grimshaw JP]]
-<ref group="xtra">PMID:19036922</ref><references group="xtra"/>
+[[Category: Malojcic G]]
-[[Category: Aryl-sulfate sulfotransferase]]
+[[Category: Owen RL]]
-[[Category: Escherichia coli]]
-[[Category: Glockshuber, R.]]
-[[Category: Grimshaw, J P.]]
-[[Category: Malojcic, G.]]
-[[Category: Owen, R L.]]
-[[Category: Bacteria]]
-[[Category: Beta propeller]]
-[[Category: Periplasm]]
-[[Category: Phenol]]
-[[Category: Protein-substrate complex]]
-[[Category: Sulfate]]
-[[Category: Transesterification]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep  3 16:01:33 2009''