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3iyh

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Revision as of 17:28, 10 April 2020

P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links

3iyh, resolution 8.20Å

Structural highlights

3iyh is a 6 chain structure with sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3iyi
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Viral 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

↑ Parent KN, Khayat R, Tu LH, Suhanovsky MM, Cortines JR, Teschke CM, Johnson JE, Baker TS. P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks. Structure. 2010 Mar 10;18(3):390-401. PMID:20223221 doi:10.1016/j.str.2009.12.014

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3iyh"

@@ Line 3: / Line 3: @@
 <SX load='3iyh' size='340' side='right' viewer='molstar' caption='[[3iyh]], [[Resolution|resolution]] 8.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3iyh]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IYH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3iyh]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IYH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3IYH FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3iyi|3iyi]]</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://pdbe.org/3iyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3iyh RCSB], [http://www.ebi.ac.uk/pdbsum/3iyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3iyh ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3iyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iyh OCA], [http://pdbe.org/3iyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3iyh RCSB], [http://www.ebi.ac.uk/pdbsum/3iyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3iyh ProSAT]</span></td></tr>
 </table>
 == Function ==

3iyh

From Proteopedia

Revision as of 17:28, 10 April 2020

P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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