3iyh: Difference between revisions
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<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=3iyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iyh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3iyh RCSB], [http://www.ebi.ac.uk/pdbsum/3iyh PDBsum]</span></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=3iyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iyh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3iyh RCSB], [http://www.ebi.ac.uk/pdbsum/3iyh PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/VG05_BPP22 VG05_BPP22]] Required for successful condensation of DNA within the capsid. Gp5 is the major structural protein of the outer shell of the prohead. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 20:44, 24 December 2014
P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-linksP22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links
Structural highlights
Function[VG05_BPP22] Required for successful condensation of DNA within the capsid. Gp5 is the major structural protein of the outer shell of the prohead. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedViral capsid assembly and stability in tailed, dsDNA phage and Herpesviridae are achieved by various means including chemical crosslinks (unique to HK97), or auxiliary proteins (lambda, T4, phi29, and herpesviruses). All these viruses have coat proteins (CP) with a conserved, HK97-like core structure. We used a combination of trypsin digestion, gold labeling, cryo-electron microscopy, 3D image reconstruction, and comparative modeling to derive two independent, pseudoatomic models of bacteriophage P22 CP: before and after maturation. P22 capsid stabilization results from intersubunit interactions among N-terminal helices and an extensive "P loop," which obviate the need for crosslinks or auxiliary proteins. P22 CP also has a telokin-like Ig domain that likely stabilizes the monomer fold so that assembly may proceed via individual subunit addition rather than via preformed capsomers as occurs in HK97. Hence, the P22 CP structure may be a paradigm for understanding how monomers assemble in viruses like phi29 and HSV-1. P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks.,Parent KN, Khayat R, Tu LH, Suhanovsky MM, Cortines JR, Teschke CM, Johnson JE, Baker TS Structure. 2010 Mar 10;18(3):390-401. PMID:20223221[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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