3c6h

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[[Image:3c6h.png|left|200px]]
 
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{{STRUCTURE_3c6h| PDB=3c6h | SCENE= }}
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==Crystal Structure of the RB49 gp17 nuclease domain==
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<StructureSection load='3c6h' size='340' side='right'caption='[[3c6h]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3c6h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB49 Escherichia phage RB49]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C6H FirstGlance]. <br>
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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]] 2.8&#8491;</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></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=3c6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6h OCA], [https://pdbe.org/3c6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c6h RCSB], [https://www.ebi.ac.uk/pdbsum/3c6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9T1C3_BPRB4 Q9T1C3_BPRB4] The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer. Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail.[HAMAP-Rule:MF_04146]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c6/3c6h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3c6h ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Viral genomes are packaged into "procapsids" by powerful molecular motors. We report the crystal structure of the DNA packaging motor protein, gene product 17 (gp17), in bacteriophage T4. The structure consists of an N-terminal ATPase domain, which provides energy for compacting DNA, and a C-terminal nuclease domain, which terminates packaging. We show that another function of the C-terminal domain is to translocate the genome into the procapsid. The two domains are in close contact in the crystal structure, representing a "tensed state." A cryo-electron microscopy reconstruction of the T4 procapsid complexed with gp17 shows that the packaging motor is a pentamer and that the domains within each monomer are spatially separated, representing a "relaxed state." These structures suggest a mechanism, supported by mutational and other data, in which electrostatic forces drive the DNA packaging by alternating between tensed and relaxed states. Similar mechanisms may occur in other molecular motors.
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===Crystal Structure of the RB49 gp17 nuclease domain===
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The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces.,Sun S, Kondabagil K, Draper B, Alam TI, Bowman VD, Zhang Z, Hegde S, Fokine A, Rossmann MG, Rao VB Cell. 2008 Dec 26;135(7):1251-62. PMID:19109896<ref>PMID:19109896</ref>
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{{ABSTRACT_PUBMED_19109896}}
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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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<div class="pdbe-citations 3c6h" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[3c6h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_rb49 Enterobacteria phage rb49]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6H OCA].
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*[[Terminase 3D Structures|Terminase 3D Structures]]
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[[Category: Enterobacteria phage rb49]]
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== References ==
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[[Category: Rossmann, M G.]]
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<references/>
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[[Category: Sun, S.]]
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__TOC__
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[[Category: Terminase nuclease]]
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</StructureSection>
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[[Category: Viral protein]]
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[[Category: Escherichia phage RB49]]
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[[Category: Large Structures]]
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[[Category: Rossmann MG]]
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[[Category: Sun S]]

Current revision

Crystal Structure of the RB49 gp17 nuclease domain

PDB ID 3c6h

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