4ar2: Difference between revisions
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==Dodecahedron formed of penton base protein from adenovirus Ad3== | |||
<StructureSection load='4ar2' size='340' side='right'caption='[[4ar2]], [[Resolution|resolution]] 3.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ar2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_adenovirus_B3 Human adenovirus B3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AR2 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]] 3.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=4ar2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ar2 OCA], [https://pdbe.org/4ar2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ar2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ar2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ar2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q2Y0H9_ADE03 Q2Y0H9_ADE03] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
During the viral life cycle adenoviruses produce excess capsid proteins. Human adenovirus serotype 3 (Ad3) synthesizes predominantly an excess of free pentons, the complexes of pentameric penton base and trimeric fiber proteins, which are responsible for virus penetration. In infected cells Ad3 pentons spontaneously assemble into dodecahedral virus-like nano-particles containing twelve pentons. They also form in insect cells during expression in the baculovirus system. Similarly, in the absence of fiber protein dodecahedric particles built of 12 penton base pentamers can be produced. Both kinds of dodecahedra show remarkable efficiency of intracellular penetration and can be engineered to deliver several millions of foreign cargo molecules to a single target cell. For this reason, they are of great interest as a delivery vector. In order to successfully manipulate this potential vector for drug and/or gene delivery, an understanding of the molecular basis of vector assembly and integrity is critical. Crystallographic data in conjunction with site-directed mutagenesis and biochemical analysis provide a model for the molecular determinants of dodecamer particle assembly and the requirements for stability. The 3.8 A crystal structure of Ad3 penton base dodecamer (Dd) shows that the dodecahedric structure is stabilized by strand-swapping between neighboring penton base molecules. Such N-terminal strand-swapping does not occur for Dd of Ad2, a serotype which does not form Dd under physiological conditions. This unique stabilization of the Ad3 dodecamer is controlled by residues 59-61 located at the site of strand switching, the residues involved in putative salt bridges between pentamers and by the disordered N-terminus (residues 1-47), as confirmed by site directed mutagenesis and biochemical analysis of mutant and wild type protein. We also provide evidence that the distal N-terminal residues are externally exposed and available for attaching cargo. | |||
The structural basis for the integrity of adenovirus ad3 dodecahedron.,Szolajska E, Burmeister WP, Zochowska M, Nerlo B, Andreev I, Schoehn G, Andrieu JP, Fender P, Naskalska A, Zubieta C, Cusack S, Chroboczek J PLoS One. 2012;7(9):e46075. doi: 10.1371/journal.pone.0046075. Epub 2012 Sep 25. PMID:23049939<ref>PMID:23049939</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ar2" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
[[Category: | == References == | ||
[[Category: Andreev | <references/> | ||
[[Category: Andrieu | __TOC__ | ||
[[Category: Burmeister | </StructureSection> | ||
[[Category: Chroboczek | [[Category: Human adenovirus B3]] | ||
[[Category: Cusack | [[Category: Large Structures]] | ||
[[Category: Fender | [[Category: Andreev I]] | ||
[[Category: Naskalska | [[Category: Andrieu J-P]] | ||
[[Category: Nerlo | [[Category: Burmeister WP]] | ||
[[Category: Schoehn | [[Category: Chroboczek J]] | ||
[[Category: Szolajska | [[Category: Cusack S]] | ||
[[Category: Zochowska | [[Category: Fender P]] | ||
[[Category: Zubieta | [[Category: Naskalska A]] | ||
[[Category: Nerlo B]] | |||
[[Category: Schoehn G]] | |||
[[Category: Szolajska E]] | |||
[[Category: Zochowska M]] | |||
[[Category: Zubieta C]] | |||
Latest revision as of 14:33, 20 December 2023
Dodecahedron formed of penton base protein from adenovirus Ad3Dodecahedron formed of penton base protein from adenovirus Ad3
Structural highlights
FunctionPublication Abstract from PubMedDuring the viral life cycle adenoviruses produce excess capsid proteins. Human adenovirus serotype 3 (Ad3) synthesizes predominantly an excess of free pentons, the complexes of pentameric penton base and trimeric fiber proteins, which are responsible for virus penetration. In infected cells Ad3 pentons spontaneously assemble into dodecahedral virus-like nano-particles containing twelve pentons. They also form in insect cells during expression in the baculovirus system. Similarly, in the absence of fiber protein dodecahedric particles built of 12 penton base pentamers can be produced. Both kinds of dodecahedra show remarkable efficiency of intracellular penetration and can be engineered to deliver several millions of foreign cargo molecules to a single target cell. For this reason, they are of great interest as a delivery vector. In order to successfully manipulate this potential vector for drug and/or gene delivery, an understanding of the molecular basis of vector assembly and integrity is critical. Crystallographic data in conjunction with site-directed mutagenesis and biochemical analysis provide a model for the molecular determinants of dodecamer particle assembly and the requirements for stability. The 3.8 A crystal structure of Ad3 penton base dodecamer (Dd) shows that the dodecahedric structure is stabilized by strand-swapping between neighboring penton base molecules. Such N-terminal strand-swapping does not occur for Dd of Ad2, a serotype which does not form Dd under physiological conditions. This unique stabilization of the Ad3 dodecamer is controlled by residues 59-61 located at the site of strand switching, the residues involved in putative salt bridges between pentamers and by the disordered N-terminus (residues 1-47), as confirmed by site directed mutagenesis and biochemical analysis of mutant and wild type protein. We also provide evidence that the distal N-terminal residues are externally exposed and available for attaching cargo. The structural basis for the integrity of adenovirus ad3 dodecahedron.,Szolajska E, Burmeister WP, Zochowska M, Nerlo B, Andreev I, Schoehn G, Andrieu JP, Fender P, Naskalska A, Zubieta C, Cusack S, Chroboczek J PLoS One. 2012;7(9):e46075. doi: 10.1371/journal.pone.0046075. Epub 2012 Sep 25. PMID:23049939[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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