View source for 4kfu


==Structure of the genome packaging NTPase B204 from Sulfolobus turreted icosahedral virus 2 in complex with AMPPCP==
<StructureSection load='4kfu' size='340' side='right'caption='[[4kfu]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kfu]] is a 4 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=4KFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KFU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.892&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4kfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfu OCA], [https://pdbe.org/4kfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kfu RCSB], [https://www.ebi.ac.uk/pdbsum/4kfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kfu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D5IEZ9_9VIRU D5IEZ9_9VIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kfu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfolobus turreted icosahedral virus 2]]
[[Category: Butcher S]]
[[Category: Goldman A]]
[[Category: Happonen LJ]]
[[Category: Kajander T]]
[[Category: Oksanen E]]