1mvm

From Proteopedia

(Difference between revisions)

Revision as of 09:30, 5 May 2021

MVM(STRAIN I), COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C

Structural highlights

1mvm is a 4 chain structure with sequence from Minute virus of mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CAPSD_MUMIM] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (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 three-dimensional crystal structure of the single-stranded DNA-containing ('full') parvovirus, minute virus of mice (MVM), has been determined to 3.5 A resolution. Both full and empty particles of MVM were crystallized in the monoclinic space group C2 with cell dimensions of a = 448.7, b = 416.7, c = 305.3 A and beta = 95.8 degrees. Diffraction data were collected at the Cornell High Energy Synchrotron Source using an oscillation camera. The crystals have a pseudo higher R32 space group in which the particles are situated at two special positions with 32 point symmetry, separated by (1/2)c in the hexagonal setting. The self-rotation function showed that the particles are rotated with respect to each other by 60 degrees around the pseudo threefold axis. Subsequently, a more detailed analysis of the structure amplitudes demonstrated that the correct space-group symmetry is C2 as given above. Only one of the three twofold axes perpendicular to the threefold axis in the pseudo R32 space group is a 'true' crystallographic twofold axis; the other two are only 'local' non-crystallographic symmetry axes. The known canine parvovirus (CPV) structure was used as a phasing model to initiate real-space electron-density averaging phase improvement. The electron density was easily interpretable and clearly showed the amino-acid differences between MVM and CPV, although the final overall correlation coefficient was only 0.63. The structure of MVM has a large amount of icosahedrally ordered DNA, amounting to 22% of the viral genome, which is significantly more than that found in CPV.

Structure determination of minute virus of mice.,Llamas-Saiz AL, Agbandje-McKenna M, Wikoff WR, Bratton J, Tattersall P, Rossmann MG Acta Crystallogr D Biol Crystallogr. 1997 Jan 1;53(Pt 1):93-102. PMID:15299974^[1]

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

References

↑ Llamas-Saiz AL, Agbandje-McKenna M, Wikoff WR, Bratton J, Tattersall P, Rossmann MG. Structure determination of minute virus of mice. Acta Crystallogr D Biol Crystallogr. 1997 Jan 1;53(Pt 1):93-102. PMID:15299974 doi:10.1107/S0907444996010566

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mvm"

@@ Line 3: / Line 3: @@
 <StructureSection load='1mvm' size='340' side='right'caption='[[1mvm]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mvm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Minute_virus_of_mice Minute virus of mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MVM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mvm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Minute_virus_of_mice Minute virus of mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVM FirstGlance]. <br>
-</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=1mvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvm OCA], [http://pdbe.org/1mvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mvm RCSB], [http://www.ebi.ac.uk/pdbsum/1mvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvm ProSAT]</span></td></tr>
+</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=1mvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvm OCA], [https://pdbe.org/1mvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvm RCSB], [https://www.ebi.ac.uk/pdbsum/1mvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CAPSD_MUMIM CAPSD_MUMIM]] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (By similarity).
+[[https://www.uniprot.org/uniprot/CAPSD_MUMIM CAPSD_MUMIM]] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Virus coat protein|Virus coat protein]]
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>

1mvm

From Proteopedia

Revision as of 09:30, 5 May 2021

MVM(STRAIN I), COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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