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2q17

From Proteopedia

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Formylglycine Generating Enzyme from Streptomyces coelicolor

Structural highlights

2q17 is a 5 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Carlson BL, Ballister ER, Skordalakes E, King DS, Breidenbach MA, Gilmore SA, Berger JM, Bertozzi CR. Function and structure of a prokaryotic formylglycine-generating enzyme. J Biol Chem. 2008 Jul 18;283(29):20117-25. Epub 2008 Apr 4. PMID:18390551 doi:10.1074/jbc.M800217200
↑ Holder PG, Jones LC, Drake PM, Barfield RM, Banas S, de Hart GW, Baker J, Rabuka D. Reconstitution of Formylglycine-generating Enzyme with Copper(II) for Aldehyde Tag Conversion. J Biol Chem. 2015 Jun 19;290(25):15730-45. doi: 10.1074/jbc.M115.652669. Epub, 2015 Apr 30. PMID:25931126 doi:http://dx.doi.org/10.1074/jbc.M115.652669
↑ Carlson BL, Ballister ER, Skordalakes E, King DS, Breidenbach MA, Gilmore SA, Berger JM, Bertozzi CR. Function and structure of a prokaryotic formylglycine-generating enzyme. J Biol Chem. 2008 Jul 18;283(29):20117-25. Epub 2008 Apr 4. PMID:18390551 doi:10.1074/jbc.M800217200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2q17"

@@ Line 1: / Line 1: @@
 ==Formylglycine Generating Enzyme from Streptomyces coelicolor==
-<StructureSection load='2q17' size='340' side='right' caption='[[2q17]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='2q17' size='340' side='right'caption='[[2q17]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2q17]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q17 FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.1&#8491;</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=2q17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q17 OCA], [http://pdbe.org/2q17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q17 RCSB], [http://www.ebi.ac.uk/pdbsum/2q17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q17 ProSAT]</span></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]]
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Strco]]
+[[Category: Large Structures]]
-[[Category: Ballister, E R]]
+[[Category: Ballister ER]]
-[[Category: Berger, J M]]
+[[Category: Berger JM]]
-[[Category: Bertozzi, C R]]
+[[Category: Bertozzi CR]]
-[[Category: Breidenbach, M A]]
+[[Category: Breidenbach MA]]
-[[Category: Carlson, B L]]
+[[Category: Carlson BL]]
-[[Category: Gilmore, S A]]
+[[Category: Gilmore SA]]
-[[Category: King, D S]]
+[[Category: King DS]]
-[[Category: Skordalakes, E]]
+[[Category: Skordalakes E]]
-[[Category: Fge]]
-[[Category: Formylglycine]]
-[[Category: Sulfatase]]
-[[Category: Unknown function]]

2q17

From Proteopedia

Current revision

Formylglycine Generating Enzyme from Streptomyces coelicolor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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