4d9j: Difference between revisions

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 ==Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains==
-<StructureSection load='4d9j' size='340' side='right' caption='[[4d9j]], [[Resolution|resolution]] 3.92&Aring;' scene=''>
+<StructureSection load='4d9j' size='340' side='right'caption='[[4d9j]], [[Resolution|resolution]] 3.92&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4d9j]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10762 Atcc 10762]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D9J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D9J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4d9j]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Puerto_Rico/8/1934(H1N1)) Influenza A virus (A/Puerto Rico/8/1934(H1N1))] and [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D9J FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vdx|3vdx]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.92&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bpoA2, BROMOPEROXIDASE A2, M, M1 Matrix ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1894 ATCC 10762])</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=4d9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d9j OCA], [https://pdbe.org/4d9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d9j RCSB], [https://www.ebi.ac.uk/pdbsum/4d9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d9j ProSAT]</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=4d9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d9j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d9j RCSB], [http://www.ebi.ac.uk/pdbsum/4d9j PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BPOA2_STRAU BPOA2_STRAU]] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis.
+[https://www.uniprot.org/uniprot/BPOA2_KITAU BPOA2_KITAU] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis.[https://www.uniprot.org/uniprot/M1_I34A1 M1_I34A1] Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.<ref>PMID:11531417</ref>   Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.<ref>PMID:11531417</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Designing protein molecules that will assemble into various kinds of ordered materials represents an important challenge in nanotechnology. We report the crystal structure of a 12-subunit protein cage that self-assembles by design to form a tetrahedral structure roughly 16 nanometers in diameter. The strategy of fusing together oligomeric protein domains can be generalized to produce other kinds of cages or extended materials.
-Structure of a 16-nm cage designed by using protein oligomers.,Lai YT, Cascio D, Yeates TO Science. 2012 Jun 1;336(6085):1129. PMID:22654051<ref>PMID:22654051</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 10762]]
+[[Category: Kitasatospora aureofaciens]]
-[[Category: Cascio, D]]
+[[Category: Large Structures]]
-[[Category: Lai, Y T]]
+[[Category: Cascio D]]
-[[Category: Yeates, T O]]
+[[Category: Lai Y-T]]
-[[Category: Biomaterial]]
+[[Category: Yeates TO]]
-[[Category: Bionanotechnology]]
-[[Category: De novo protein]]
-[[Category: Protein assembly]]
-[[Category: Protein design]]
-[[Category: Symmetry]]