1dml

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[[Image:1dml.gif|left|200px]]<br /><applet load="1dml" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dml, resolution 2.70&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL==
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Herpes simplex virus DNA polymerase is a heterodimer composed of a catalytic subunit, Pol, and an unusual processivity subunit, UL42, which, unlike processivity factors such as PCNA, directly binds DNA. The crystal structure of a complex of the C-terminal 36 residues of Pol bound to residues 1-319 of UL42 reveals remarkable similarities between UL42 and PCNA despite contrasting biochemical properties and lack of sequence homology. Moreover, the Pol-UL42 interaction resembles the interaction between the cell cycle regulator p21 and PCNA. The structure and previous data suggest that the UL42 monomer interacts with DNA quite differently than does multimeric toroidal PCNA. The details of the structure lead to a model for the mechanism of UL42, provide the basis for drug design, and allow modeling of other proteins that lack sequence homology with UL42 or PCNA.
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<StructureSection load='1dml' size='340' side='right'caption='[[1dml]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1dml]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1 Human alphaherpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DML FirstGlance]. <br>
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1DML is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DML OCA].
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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]] 2.7&#8491;</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=1dml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dml OCA], [https://pdbe.org/1dml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dml RCSB], [https://www.ebi.ac.uk/pdbsum/1dml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dml ProSAT]</span></td></tr>
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==Reference==
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</table>
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The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase., Zuccola HJ, Filman DJ, Coen DM, Hogle JM, Mol Cell. 2000 Feb;5(2):267-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10882068 10882068]
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== Function ==
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[[Category: DNA-directed DNA polymerase]]
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[https://www.uniprot.org/uniprot/PAP_HHV11 PAP_HHV11] Plays an essential role in viral DNA replication by acting as the polymerase accessory subunit. Associates with the viral polymerase to increase its processivity and forms high-affinity direct interactions with DNA. Facilitates the origin-binding protein UL9 loading onto DNA thus increasing its ability to assemble into a functional complex capable of unwinding duplex DNA.<ref>PMID:2173776</ref>
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[[Category: Human herpesvirus 4]]
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== Evolutionary Conservation ==
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[[Category: Protein complex]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Coen, D M.]]
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Check<jmol>
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[[Category: Filman, D J.]]
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<jmolCheckbox>
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[[Category: Hogle, J M.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dm/1dml_consurf.spt"</scriptWhenChecked>
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[[Category: Zuccola, H J.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: dna synthesis]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: herpes simplex virus]]
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</jmolCheckbox>
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[[Category: pcna]]
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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=1dml ConSurf].
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[[Category: processivity]]
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<div style="clear:both"></div>
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[[Category: sliding clamps]]
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== References ==
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<references/>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:17 2008''
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__TOC__
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</StructureSection>
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[[Category: Human alphaherpesvirus 1]]
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[[Category: Large Structures]]
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[[Category: Coen DM]]
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[[Category: Filman DJ]]
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[[Category: Hogle JM]]
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[[Category: Zuccola HJ]]

Current revision

CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL

PDB ID 1dml

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