This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5e9t

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:22, 21 October 2020

Crystal structure of GtfA/B complex

Structural highlights

5e9t is a 4 chain structure with sequence from Atcc 10558. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	5e9u
Gene:	gtf1, gtfA (ATCC 10558), gtf2, gtfB (ATCC 10558)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GTF1_STRGN] An N-acetylglucosaminyl transferase that is part of the accessory SecA2/SecY2 system specifically required to export GspB, a serine-rich repeat cell wall protein usually encoded upstream in the same operon. Required for correct glycosylation of GspB. Upon coexpression in E.coli with Gtf2 (GtfB) glycosylates GspB constructs. Glycosylation probably occurs intracellularly.^[1] [GTF2_STRGN] A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export GspB, a serine-rich repeat cell wall protein encoded upstream in the same operon. Required for correct glycosylation of GspB. Upon coexpression in E.coli with Gtf1 (GtfA) glycosylates GspB constructs. Stabilizes the glycosylation activity of Gtf1 (By similarity).^[2]

Publication Abstract from PubMed

O-glycosylation of Ser and Thr residues is an important process in all organisms, which is only poorly understood. Such modification is required for the export and function of adhesin proteins that mediate the attachment of pathogenic Gram-positive bacteria to host cells. Here, we have analyzed the mechanism by which the cytosolic O-glycosyltransferase GtfA/B of Streptococcus gordonii modifies the Ser/Thr-rich repeats of adhesin. The enzyme is a tetramer containing two molecules each of GtfA and GtfB. The two subunits have the same fold, but only GtfA contains an active site, whereas GtfB provides the primary binding site for adhesin. During a first phase of glycosylation, the conformation of GtfB is restrained by GtfA to bind substrate with unmodified Ser/Thr residues. In a slow second phase, GtfB recognizes residues that are already modified with N-acetylglucosamine, likely by converting into a relaxed conformation in which one interface with GtfA is broken. These results explain how the glycosyltransferase modifies a progressively changing substrate molecule.

Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein.,Chen Y, Seepersaud R, Bensing BA, Sullam PM, Rapoport TA Proc Natl Acad Sci U S A. 2016 Feb 16. pii: 201600494. PMID:26884191^[3]

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

References

↑ Takamatsu D, Bensing BA, Sullam PM. Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii mediate the intracellular glycosylation of the platelet-binding protein GspB. J Bacteriol. 2004 Nov;186(21):7100-11. PMID:15489421 doi:http://dx.doi.org/186/21/7100
↑ Takamatsu D, Bensing BA, Sullam PM. Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii mediate the intracellular glycosylation of the platelet-binding protein GspB. J Bacteriol. 2004 Nov;186(21):7100-11. PMID:15489421 doi:http://dx.doi.org/186/21/7100
↑ Chen Y, Seepersaud R, Bensing BA, Sullam PM, Rapoport TA. Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein. Proc Natl Acad Sci U S A. 2016 Feb 16. pii: 201600494. PMID:26884191 doi:http://dx.doi.org/10.1073/pnas.1600494113

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5e9t"

@@ Line 3: / Line 3: @@
 <StructureSection load='5e9t' size='340' side='right'caption='[[5e9t]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5e9t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10558 Atcc 10558]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E9T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5e9t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10558 Atcc 10558]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E9T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E9T FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e9u|5e9u]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gtf1, gtfA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1302 ATCC 10558]), gtf2, gtfB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1302 ATCC 10558])</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=5e9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e9t OCA], [http://pdbe.org/5e9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e9t RCSB], [http://www.ebi.ac.uk/pdbsum/5e9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e9t ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e9t OCA], [http://pdbe.org/5e9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e9t RCSB], [http://www.ebi.ac.uk/pdbsum/5e9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e9t ProSAT]</span></td></tr>
 </table>
 == Function ==

5e9t

From Proteopedia

Revision as of 08:22, 21 October 2020

Crystal structure of GtfA/B complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox