1mec

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Revision as of 10:09, 25 October 2017

CONFORMATIONAL VARIABILITY OF A PICORNAVIRUS CAPSID: PH-DEPENDENT STRUCTURAL CHANGES OF MENGO VIRUS RELATED TO ITS HOST RECEPTOR ATTACHMENT SITE AND DISASSEMBLY

Structural highlights

1mec is a 4 chain structure with sequence from Enmgo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[POLG_ENMGO] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). Protein VP0: VP0 precursor is a component of immature procapsids (By similarity). Protein 2B: Affects membrane integrity and cause an increase in membrane permeability (By similarity). Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity). Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity). RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity). Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function (By similarity).

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 PubMed

The structure of Mengo virus had been determined from crystals grown in the presence of 100 mM phosphate buffer at pH 7.4. It is shown that Mengo virus is poorly infectious at the phosphate concentration similar to that in which it was crystallized. Maximal infectivity is achieved at 10 mM phosphate or less in physiological saline. The phosphate effect is ameliorated when the pH is lowered to 4.6. Although it has not been possible to study the crystal structure of the virus at low phosphate concentrations, it is shown that increasing the Cl- concentration at pH 6.2 or decreasing the pH to 4.6 causes substantial conformational changes confined to the "pit," a deep surface depression. These structural changes involve a movement of the "FMDV loop" (GH loop) in VP1, an ordering of the "VP3 loop" (GH loop in VP3) between 3176 and 3182, the displacement of a bound phosphate near the "FMDV loop" (GH loop in VP1), and movement of the carboxy terminus of VP2. The changes in conformation are correlated with the dissociation of the virion into pentamers at pH 6.2 and 150 mM Cl-. The localization of the conformational changes and the correlated role of the phosphate in controlling infectivity support the hypothesis that the "pit" is the receptor attachment site.

Conformational variability of a picornavirus capsid: pH-dependent structural changes of Mengo virus related to its host receptor attachment site and disassembly.,Kim S, Boege U, Krishnaswamy S, Minor I, Smith TJ, Luo M, Scraba DG, Rossmann MG Virology. 1990 Mar;175(1):176-90. PMID:2155508^[1]

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

References

↑ Kim S, Boege U, Krishnaswamy S, Minor I, Smith TJ, Luo M, Scraba DG, Rossmann MG. Conformational variability of a picornavirus capsid: pH-dependent structural changes of Mengo virus related to its host receptor attachment site and disassembly. Virology. 1990 Mar;175(1):176-90. PMID:2155508

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/1mec"

Categories: Enmgo | Rossmann, M G | Cardio picornavirus coat protein | Icosahedral virus | Virus

@@ Line 1: / Line 1: @@
 ==CONFORMATIONAL VARIABILITY OF A PICORNAVIRUS CAPSID: PH-DEPENDENT STRUCTURAL CHANGES OF MENGO VIRUS RELATED TO ITS HOST RECEPTOR ATTACHMENT SITE AND DISASSEMBLY==
 <StructureSection load='1mec' size='340' side='right' caption='[[1mec]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1mec]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enmgo Enmgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MEC FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1mec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mec OCA], [http://pdbe.org/1mec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mec RCSB], [http://www.ebi.ac.uk/pdbsum/1mec 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=1mec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mec OCA], [http://pdbe.org/1mec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mec RCSB], [http://www.ebi.ac.uk/pdbsum/1mec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mec ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mec ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1mec" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Virus coat protein|Virus coat protein]]
 == References ==
 <references/>

1mec

From Proteopedia

Revision as of 10:09, 25 October 2017

CONFORMATIONAL VARIABILITY OF A PICORNAVIRUS CAPSID: PH-DEPENDENT STRUCTURAL CHANGES OF MENGO VIRUS RELATED TO ITS HOST RECEPTOR ATTACHMENT SITE AND DISASSEMBLY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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