6yus

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:46, 23 October 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='6yus' size='340' side='right'caption='[[6yus]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6yus' size='340' side='right'caption='[[6yus]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6yus]] 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=6YUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YUS FirstGlance]. <br>
+
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YUS 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]] 2&#8491;</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=OAS:O-ACETYLSERINE'>OAS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=OAS:O-ACETYLSERINE'>OAS</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=6yus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yus OCA], [https://pdbe.org/6yus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yus RCSB], [https://www.ebi.ac.uk/pdbsum/6yus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yus ProSAT]</span></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=6yus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yus OCA], [https://pdbe.org/6yus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yus RCSB], [https://www.ebi.ac.uk/pdbsum/6yus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yus ProSAT]</span></td></tr>
</table>
</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 6yus" style="background-color:#fffaf0;"></div>
 
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Neisseria meningitidis serogroup A]]
 
[[Category: Cramer JT]]
[[Category: Cramer JT]]
[[Category: Fedorov R]]
[[Category: Fedorov R]]
[[Category: Fiebig T]]
[[Category: Fiebig T]]
[[Category: Muehlenhoff M]]
[[Category: Muehlenhoff M]]

Current revision

Capsule O-acetyltransferase of Neisseria meningitidis serogroup A H228A mutant in complex with CoA

PDB ID 6yus

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools