3cpe

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{{Seed}}
 
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[[Image:3cpe.jpg|left|200px]]
 
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==Crystal Structure of T4 gp17==
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The line below this paragraph, containing "STRUCTURE_3cpe", creates the "Structure Box" on the page.
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<StructureSection load='3cpe' size='340' side='right'caption='[[3cpe]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3cpe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CPE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_3cpe| PDB=3cpe | SCENE= }}
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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=3cpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cpe OCA], [https://pdbe.org/3cpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cpe RCSB], [https://www.ebi.ac.uk/pdbsum/3cpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cpe ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TERL_BPT4 TERL_BPT4] Component of the molecular motor that translocates genomic DNA in empty capsid during DNA packaging. Heterodimerizes with small terminase protein to be docked on capsid portal protein. The latter forms a ring in which genomic DNA in translocated into the capsid. May have or induce an endonuclease activity to cleave the genome concatemer after encapsidation (By similarity).
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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/cp/3cpe_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=3cpe 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 T4 gp17===
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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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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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The line below this paragraph, {{ABSTRACT_PUBMED_19109896}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3cpe" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19109896 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19109896}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia virus T4]]
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3CPE is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CPE OCA].
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[[Category: Large Structures]]
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[[Category: Rossmann MG]]
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==Reference==
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[[Category: Sun S]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/19109896 19109896]
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[[Category: Enterobacteria phage t4]]
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[[Category: Rossmann, M G.]]
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[[Category: Sun, S.]]
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[[Category: Alternative initiation]]
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[[Category: Atp-binding]]
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[[Category: Dna-binding]]
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[[Category: Hydrolase]]
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[[Category: Large terminase]]
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[[Category: Nuclease]]
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[[Category: Nucleotide-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 14 13:13:09 2009''
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Current revision

Crystal Structure of T4 gp17

PDB ID 3cpe

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