2q17
From Proteopedia
(Difference between revisions)
| (14 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2q17.jpg|left|200px]] | ||
| - | < | + | ==Formylglycine Generating Enzyme from Streptomyces coelicolor== |
| - | + | <StructureSection load='2q17' size='340' side='right'caption='[[2q17]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | or the | + | <table><tr><td colspan='2'>[[2q17]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q17 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]] 2.1Å</td></tr> | |
| - | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=2q17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q17 OCA], [https://pdbe.org/2q17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q17 RCSB], [https://www.ebi.ac.uk/pdbsum/2q17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q17 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FGE_STRCO FGE_STRCO] Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile.<ref>PMID:18390551</ref> <ref>PMID:25931126</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/q1/2q17_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=2q17 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Type I sulfatases require an unusual co- or post-translational modification for their activity in hydrolyzing sulfate esters. In eukaryotic sulfatases, an active site cysteine residue is oxidized to the aldehyde-containing C(alpha)-formylglycine residue by the formylglycine-generating enzyme (FGE). The machinery responsible for sulfatase activation is poorly understood in prokaryotes. Here we describe the identification of a prokaryotic FGE from Mycobacterium tuberculosis. In addition, we solved the crystal structure of the Streptomyces coelicolor FGE homolog to 2.1 A resolution. The prokaryotic homolog exhibits remarkable structural similarity to human FGE, including the position of catalytic cysteine residues. Both biochemical and structural data indicate the presence of an oxidized cysteine modification in the active site that may be relevant to catalysis. In addition, we generated a mutant M. tuberculosis strain lacking FGE. Although global sulfatase activity was reduced in the mutant, a significant amount of residual sulfatase activity suggests the presence of FGE-independent sulfatases in this organism. | ||
| - | + | Function and structure of a prokaryotic formylglycine-generating enzyme.,Carlson BL, Ballister ER, Skordalakes E, King DS, Breidenbach MA, Gilmore SA, Berger JM, Bertozzi CR J Biol Chem. 2008 Jul 18;283(29):20117-25. Epub 2008 Apr 4. PMID:18390551<ref>PMID:18390551</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2q17" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Ballister | + | __TOC__ |
| - | [[Category: Berger | + | </StructureSection> |
| - | [[Category: Bertozzi | + | [[Category: Large Structures]] |
| - | [[Category: Breidenbach | + | [[Category: Ballister ER]] |
| - | [[Category: Carlson | + | [[Category: Berger JM]] |
| - | [[Category: Gilmore | + | [[Category: Bertozzi CR]] |
| - | [[Category: King | + | [[Category: Breidenbach MA]] |
| - | [[Category: Skordalakes | + | [[Category: Carlson BL]] |
| - | + | [[Category: Gilmore SA]] | |
| - | + | [[Category: King DS]] | |
| - | + | [[Category: Skordalakes E]] | |
| - | + | ||
| - | + | ||
Current revision
Formylglycine Generating Enzyme from Streptomyces coelicolor
| |||||||||||
