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4kfr

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==Structure of the genome packaging NTPase B204 from Sulfolobus turreted icosahedral virus 2 in complex with sulfate==
==Structure of the genome packaging NTPase B204 from Sulfolobus turreted icosahedral virus 2 in complex with sulfate==
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<StructureSection load='4kfr' size='340' side='right' caption='[[4kfr]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
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<StructureSection load='4kfr' size='340' side='right'caption='[[4kfr]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4kfr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_turreted_icosahedral_virus_2 Sulfolobus turreted icosahedral virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KFR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4kfr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_turreted_icosahedral_virus_2 Sulfolobus turreted icosahedral virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KFR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.956&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kfs|4kfs]], [[4kft|4kft]], [[4kfu|4kfu]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B204, STIV2_B204 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=754004 Sulfolobus turreted icosahedral virus 2])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfr OCA], [https://pdbe.org/4kfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kfr RCSB], [https://www.ebi.ac.uk/pdbsum/4kfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kfr ProSAT]</span></td></tr>
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<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=4kfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kfr RCSB], [http://www.ebi.ac.uk/pdbsum/4kfr PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/D5IEZ9_9VIRU D5IEZ9_9VIRU]
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Biochemical reactions powered by ATP hydrolysis are fundamental for the movement of molecules and cellular structures. One such reaction is the encapsidation of the dsDNA genome of an icosahedrally-symmetric virus into a preformed procapsid with the help of a genome translocating NTPase. Such NTPases have been characterized in detail from both RNA and tailed DNA viruses. We present four crystal structures and the biochemical activity of a thermophilic NTPase, B204, from the non-tailed, membrane-containing, hyperthermo-acidophilic archaeal dsDNA virus Sulfolobus turreted icosahedral virus 2. These are the first structures of a genome packaging NTPase from a non-tailed, dsDNA virus with an archaeal host. The four structures highlight the catalytic cycle of B204, pinpointing the molecular movement between substrate-bound (open) and empty (closed) active sites. The protein is shown to bind both single-stranded and double-stranded nucleic acids, and to have an optimum activity at 80 degrees C and pH 4.5. The overall fold of B204 places it in the FtsK-HerA superfamily of P-loop ATPases, whose cellular and viral members have been suggested to share a common DNA-translocating mechanism.
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The structure of the NTPase that powers DNA packaging into Sulfolobus turreted icosahedral virus 2.,Happonen LJ, Oksanen E, Liljeroos L, Goldman A, Kajander T, Butcher SJ J Virol. 2013 May 22. PMID:23698307<ref>PMID:23698307</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Sulfolobus turreted icosahedral virus 2]]
[[Category: Sulfolobus turreted icosahedral virus 2]]
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[[Category: Butcher, S]]
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[[Category: Butcher S]]
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[[Category: Goldman, A]]
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[[Category: Goldman A]]
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[[Category: Happonen, L J]]
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[[Category: Happonen LJ]]
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[[Category: Kajander, T]]
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[[Category: Kajander T]]
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[[Category: Oksanen, E]]
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[[Category: Oksanen E]]
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[[Category: Ftsk-hera superfamily]]
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[[Category: Genome packaging ntpase]]
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[[Category: Hydrolase]]
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[[Category: P-loop atpase]]
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Current revision

Structure of the genome packaging NTPase B204 from Sulfolobus turreted icosahedral virus 2 in complex with sulfate

PDB ID 4kfr

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