1mvm: Difference between revisions

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-[[Image:1mvm.gif|left|200px]]
- {{Structure
+==MVM(STRAIN I), COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C==
-|PDB= 1mvm |SIZE=350|CAPTION= <scene name='initialview01'>1mvm</scene>, resolution 3.500&Aring;
+<StructureSection load='1mvm' size='340' side='right'caption='[[1mvm]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<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>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
-|GENE=
+<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 ==
+[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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mv/1mvm_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <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/main_output.php?pdb_ID=1mvm ConSurf].
+<div style="clear:both"></div>
-'''MVM(STRAIN I), COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C'''
+==See Also==
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
-==About this Structure==
-MVM is a [[Single protein]] structure of 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].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/15299974 15299974]
 [[Category: Minute virus of mice]]
-[[Category: Single protein]]
+[[Category: Agbandje-McKenna M]]
-[[Category: Agbandje-McKenna, M.]]
+[[Category: Llamas-Saiz AL]]
-[[Category: Llamas-Saiz, M G.Rossmann A L.]]
+[[Category: Rossmann MG]]
-[[Category: complex (viral coat protein/dna)]]
-[[Category: icosahedral virus]]
-[[Category: viral coat protein/nucleic acid]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:48:45 2008''