6yuv: Difference between revisions
New page: '''Unreleased structure''' The entry 6yuv is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Capsule O-acetyltransferase of Neisseria meningitidis serogroup A== | |||
<StructureSection load='6yuv' size='340' side='right'caption='[[6yuv]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6yuv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_A Neisseria meningitidis serogroup A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YUV 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=6yuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yuv OCA], [https://pdbe.org/6yuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yuv RCSB], [https://www.ebi.ac.uk/pdbsum/6yuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yuv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O68216_NEIMD O68216_NEIMD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
O-Acetylation of the capsular polysaccharide (CPS) of Neisseria meningitidis serogroup A (NmA) is critical for the induction of functional immune responses, making this modification mandatory for CPS-based anti-NmA vaccines. Using comprehensive NMR studies, we demonstrate that O-acetylation stabilizes the labile anomeric phosphodiester-linkages of the NmA-CPS and occurs in position C3 and C4 of the N-acetylmannosamine units due to enzymatic transfer and non-enzymatic ester migration, respectively. To shed light on the enzymatic transfer mechanism, we solved the crystal structure of the capsule O-acetyltransferase CsaC in its apo and acceptor-bound form and of the CsaC-H228A mutant as trapped acetyl-enzyme adduct in complex with CoA. Together with the results of a comprehensive mutagenesis study, the reported structures explain the strict regioselectivity of CsaC and provide insight into the catalytic mechanism, which relies on an unexpected Gln-extension of a classical Ser-His-Asp triad, embedded in an alpha/beta-hydrolase fold. | |||
Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A.,Fiebig T, Cramer JT, Bethe A, Baruch P, Curth U, Fuhring JI, Buettner FFR, Vogel U, Schubert M, Fedorov R, Muhlenhoff M Nat Commun. 2020 Sep 18;11(1):4723. doi: 10.1038/s41467-020-18464-y. PMID:32948778<ref>PMID:32948778</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6yuv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neisseria meningitidis serogroup A]] | |||
[[Category: Cramer JT]] | |||
[[Category: Fedorov R]] | |||
[[Category: Fiebig T]] | |||
[[Category: Muehlenhoff M]] | |||
Latest revision as of 16:36, 24 January 2024
Capsule O-acetyltransferase of Neisseria meningitidis serogroup ACapsule O-acetyltransferase of Neisseria meningitidis serogroup A
Structural highlights
FunctionPublication Abstract from PubMedO-Acetylation of the capsular polysaccharide (CPS) of Neisseria meningitidis serogroup A (NmA) is critical for the induction of functional immune responses, making this modification mandatory for CPS-based anti-NmA vaccines. Using comprehensive NMR studies, we demonstrate that O-acetylation stabilizes the labile anomeric phosphodiester-linkages of the NmA-CPS and occurs in position C3 and C4 of the N-acetylmannosamine units due to enzymatic transfer and non-enzymatic ester migration, respectively. To shed light on the enzymatic transfer mechanism, we solved the crystal structure of the capsule O-acetyltransferase CsaC in its apo and acceptor-bound form and of the CsaC-H228A mutant as trapped acetyl-enzyme adduct in complex with CoA. Together with the results of a comprehensive mutagenesis study, the reported structures explain the strict regioselectivity of CsaC and provide insight into the catalytic mechanism, which relies on an unexpected Gln-extension of a classical Ser-His-Asp triad, embedded in an alpha/beta-hydrolase fold. Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A.,Fiebig T, Cramer JT, Bethe A, Baruch P, Curth U, Fuhring JI, Buettner FFR, Vogel U, Schubert M, Fedorov R, Muhlenhoff M Nat Commun. 2020 Sep 18;11(1):4723. doi: 10.1038/s41467-020-18464-y. PMID:32948778[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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