4ncw

From Proteopedia

(Difference between revisions)

Current revision

foldon domain wild type C-conjugate

Structural highlights

4ncw is a 3 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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').

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^[1]

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

References

↑ Berthelmann A, Lach J, Grawert MA, Groll M, Eichler J. Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimer. Org Biomol Chem. 2014 Apr 28;12(16):2606-14. doi: 10.1039/c3ob42251h. PMID:24637609 doi:http://dx.doi.org/10.1039/c3ob42251h

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/4ncw"

@@ Line 1: / Line 1: @@
 ==foldon domain wild type C-conjugate==
-<StructureSection load='4ncw' size='340' side='right' caption='[[4ncw]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
+<StructureSection load='4ncw' size='340' side='right'caption='[[4ncw]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ncw]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NCW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ncw]] 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=4NCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NCW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2KN:N,N,N-TRIETHYLBENZENE-1,3,5-TRICARBOXAMIDE'>2KN</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]] 1.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rfo|1rfo]], [[4ncu|4ncu]], [[4ncv|4ncv]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2KN:N,N,N-TRIETHYLBENZENE-1,3,5-TRICARBOXAMIDE'>2KN</scene></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=4ncw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ncw OCA], [http://pdbe.org/4ncw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ncw RCSB], [http://www.ebi.ac.uk/pdbsum/4ncw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ncw 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=4ncw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ncw OCA], [https://pdbe.org/4ncw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ncw RCSB], [https://www.ebi.ac.uk/pdbsum/4ncw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ncw 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 ==
@@ Line 24: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Berthelmann, A]]
+[[Category: Escherichia virus T4]]
-[[Category: Eichler, J]]
+[[Category: Large Structures]]
-[[Category: Graewert, M A]]
+[[Category: Berthelmann A]]
-[[Category: Groll, M]]
+[[Category: Eichler J]]
-[[Category: Lach, J]]
+[[Category: Graewert MA]]
-[[Category: Chemical ligation]]
+[[Category: Groll M]]
-[[Category: Folding]]
+[[Category: Lach J]]
-[[Category: Trazido-functionalized trimesic acid scaffold]]
-[[Category: Trimeric scaffold]]
-[[Category: Viral protein]]

4ncw

From Proteopedia

Current revision

foldon domain wild type C-conjugate

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