4ncv: Difference between revisions
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==Foldon domain wild type N-conjugate== | |||
<StructureSection load='4ncv' size='340' side='right'caption='[[4ncv]], [[Resolution|resolution]] 1.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ncv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NCV 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]] 1.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=4ncv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ncv OCA], [https://pdbe.org/4ncv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ncv RCSB], [https://www.ebi.ac.uk/pdbsum/4ncv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ncv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers'). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
C3-Symmetric trimesic acid scaffolds, functionalized with bromoacetyl, aminooxyacetyl and azidoacetyl moieties, respectively, were synthesized and compared regarding their utility for the trivalent presentation of peptides using three different chemoselective ligation reactions, i.e. thioether and oxime formation, as well as the "click" reaction. The latter ligation method was then used to covalently stabilize the trimer of foldon, a 27 amino acid trimerization domain of bacteriophage T4 fibritin, by linking the three foldon monomers to the triazido-functionalized trimesic acid scaffold. This reaction dramatically enhanced the thermal stability of the trimer, while maintaining the correct fold, as demonstrated by CD spectroscopy and X-ray crystal structure analysis, respectively, of the foldon-scaffold conjugates. | |||
Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimer.,Berthelmann A, Lach J, Grawert MA, Groll M, Eichler J Org Biomol Chem. 2014 Apr 28;12(16):2606-14. doi: 10.1039/c3ob42251h. PMID:24637609<ref>PMID:24637609</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ncv" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Fibritin|Fibritin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia virus T4]] | |||
[[Category: Large Structures]] | |||
[[Category: Berthelmann A]] | |||
[[Category: Eichler J]] | |||
[[Category: Graewert MA]] | |||
[[Category: Groll M]] | |||
[[Category: Lach J]] | |||
Latest revision as of 19:53, 20 September 2023
Foldon domain wild type N-conjugateFoldon domain wild type N-conjugate
Structural highlights
FunctionWAC_BPT4 Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers'). Publication Abstract from PubMedC3-Symmetric trimesic acid scaffolds, functionalized with bromoacetyl, aminooxyacetyl and azidoacetyl moieties, respectively, were synthesized and compared regarding their utility for the trivalent presentation of peptides using three different chemoselective ligation reactions, i.e. thioether and oxime formation, as well as the "click" reaction. The latter ligation method was then used to covalently stabilize the trimer of foldon, a 27 amino acid trimerization domain of bacteriophage T4 fibritin, by linking the three foldon monomers to the triazido-functionalized trimesic acid scaffold. This reaction dramatically enhanced the thermal stability of the trimer, while maintaining the correct fold, as demonstrated by CD spectroscopy and X-ray crystal structure analysis, respectively, of the foldon-scaffold conjugates. Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimer.,Berthelmann A, Lach J, Grawert MA, Groll M, Eichler J Org Biomol Chem. 2014 Apr 28;12(16):2606-14. doi: 10.1039/c3ob42251h. PMID:24637609[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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