2q17

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{{Seed}}
 
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[[Image:2q17.png|left|200px]]
 
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==Formylglycine Generating Enzyme from Streptomyces coelicolor==
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The line below this paragraph, containing "STRUCTURE_2q17", creates the "Structure Box" on the page.
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<StructureSection load='2q17' size='340' side='right'caption='[[2q17]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<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>
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{{STRUCTURE_2q17| PDB=2q17 | SCENE= }}
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q1/2q17_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Formylglycine Generating Enzyme from Streptomyces coelicolor===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_18390551}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2q17" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18390551 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18390551}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2Q17 is a 5 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q17 OCA].
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[[Category: Ballister ER]]
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[[Category: Berger JM]]
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==Reference==
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[[Category: Bertozzi CR]]
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<ref group="xtra">PMID:18390551</ref><references group="xtra"/>
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[[Category: Breidenbach MA]]
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[[Category: Bacteria]]
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[[Category: Carlson BL]]
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[[Category: Ballister, E R.]]
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[[Category: Gilmore SA]]
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[[Category: Berger, J M.]]
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[[Category: King DS]]
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[[Category: Bertozzi, C R.]]
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[[Category: Skordalakes E]]
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[[Category: Breidenbach, M A.]]
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[[Category: Carlson, B L.]]
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[[Category: Gilmore, S A.]]
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[[Category: King, D S.]]
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[[Category: Skordalakes, E.]]
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[[Category: Fge]]
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[[Category: Formylglycine]]
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[[Category: Sulfatase]]
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[[Category: Unknown function]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:16:28 2009''
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Current revision

Formylglycine Generating Enzyme from Streptomyces coelicolor

PDB ID 2q17

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