4wac: Difference between revisions
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==Crystal Structure of TarM== | ==Crystal Structure of TarM== | ||
<StructureSection load='4wac' size='340' side='right' caption='[[4wac]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4wac' size='340' side='right'caption='[[4wac]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wac]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WAC OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4wac]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WAC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.4Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4wac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wac OCA], [https://pdbe.org/4wac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wac RCSB], [https://www.ebi.ac.uk/pdbsum/4wac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wac ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0D6HUA0_STAAU A0A0D6HUA0_STAAU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Anionic glycopolymers known as wall teichoic acids (WTAs) functionalize the peptidoglycan layers of many Gram-positive bacteria. WTAs play central roles in many fundamental aspects of bacterial physiology, and they are important determinants of pathogenesis and antibiotic resistance. A number of enzymes that glycosylate WTA in S. aureus have recently been identified. Among these is the glycosyltransferase TarM, a component of the WTA de-novo biosynthesis pathway. TarM performs the synthesis of alpha-O-N-acetylglycosylated poly-5'-phosphoribitol in the WTA structure. We have solved the crystal structure of TarM at 2.4 A resolution, and we have also determined a structure of the enzyme in complex with its substrate UDP-GlcNAc at 2.8 A resolution. The protein assembles into a propeller-like homotrimer, in which each blade contains a GT-B-type glycosyltransferase domain with a typical Rossmann fold. The enzymatic reaction retains the stereochemistry of the anomeric center of the transferred GlcNAc-moiety on the polyribitol backbone. TarM assembles into a trimer using a novel trimerization domain, here termed the HUB domain. Structure-guided mutagenesis experiments of TarM identify residues critical for enzyme activity, assign a putative role for the HUB in TarM function, and allow us to propose a likely reaction mechanism. | |||
Structural and enzymatic analysis of TarM from Staphylococcus aureus reveals an oligomeric protein specific for the glycosylation of wall teichoic acid.,Koc C, Gerlach D, Beck S, Peschel A, Xia G, Stehle T J Biol Chem. 2015 Feb 19. pii: jbc.M114.619924. PMID:25697358<ref>PMID:25697358</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4wac" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: | [[Category: Koc C]] | ||
[[Category: | [[Category: Peschel A]] | ||
[[Category: | [[Category: Stehle T]] | ||
[[Category: | [[Category: Xia G]] | ||
Latest revision as of 14:27, 9 May 2024
Crystal Structure of TarMCrystal Structure of TarM
Structural highlights
FunctionPublication Abstract from PubMedAnionic glycopolymers known as wall teichoic acids (WTAs) functionalize the peptidoglycan layers of many Gram-positive bacteria. WTAs play central roles in many fundamental aspects of bacterial physiology, and they are important determinants of pathogenesis and antibiotic resistance. A number of enzymes that glycosylate WTA in S. aureus have recently been identified. Among these is the glycosyltransferase TarM, a component of the WTA de-novo biosynthesis pathway. TarM performs the synthesis of alpha-O-N-acetylglycosylated poly-5'-phosphoribitol in the WTA structure. We have solved the crystal structure of TarM at 2.4 A resolution, and we have also determined a structure of the enzyme in complex with its substrate UDP-GlcNAc at 2.8 A resolution. The protein assembles into a propeller-like homotrimer, in which each blade contains a GT-B-type glycosyltransferase domain with a typical Rossmann fold. The enzymatic reaction retains the stereochemistry of the anomeric center of the transferred GlcNAc-moiety on the polyribitol backbone. TarM assembles into a trimer using a novel trimerization domain, here termed the HUB domain. Structure-guided mutagenesis experiments of TarM identify residues critical for enzyme activity, assign a putative role for the HUB in TarM function, and allow us to propose a likely reaction mechanism. Structural and enzymatic analysis of TarM from Staphylococcus aureus reveals an oligomeric protein specific for the glycosylation of wall teichoic acid.,Koc C, Gerlach D, Beck S, Peschel A, Xia G, Stehle T J Biol Chem. 2015 Feb 19. pii: jbc.M114.619924. PMID:25697358[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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