1t6l: Difference between revisions

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<StructureSection load='1t6l' size='340' side='right'caption='[[1t6l]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='1t6l' size='340' side='right'caption='[[1t6l]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1t6l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hcmv Hcmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1T6L FirstGlance]. <br>
<table><tr><td colspan='2'>[[1t6l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betaherpesvirus_5 Human betaherpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T6L FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UL44 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10359 HCMV])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1t6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t6l OCA], [http://pdbe.org/1t6l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t6l RCSB], [http://www.ebi.ac.uk/pdbsum/1t6l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t6l ProSAT]</span></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=1t6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t6l OCA], [https://pdbe.org/1t6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t6l RCSB], [https://www.ebi.ac.uk/pdbsum/1t6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t6l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VPAP_HCMVA VPAP_HCMVA]] Accessory subunit of the DNA polymerase that acts to increase the processivity of polymerization.<ref>PMID:20538862</ref>
[https://www.uniprot.org/uniprot/VPAP_HCMVA VPAP_HCMVA] Accessory subunit of the DNA polymerase that acts to increase the processivity of polymerization.<ref>PMID:20538862</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1t6l ConSurf].
</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=1t6l ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human cytomegalovirus DNA polymerase consists of a catalytic subunit, UL54, and a presumed processivity factor, UL44. We have solved the crystal structure of residues 1-290 of UL44 to 1.85 A resolution by multiwavelength anomalous dispersion. The structure reveals a dimer of UL44 in the shape of a C clamp. Each monomer of UL44 shares its overall fold with other processivity factors, including herpes simplex virus UL42, which is a monomer that binds DNA directly, and the sliding clamp, PCNA, which is a trimer that surrounds DNA, although these proteins share no obvious sequence homology. Analytical ultracentrifugation and gel filtration measurements demonstrated that UL44 also forms a dimer in solution, and substitution of large hydrophobic residues along the homodimer interface with alanine disrupted dimerization and decreased DNA binding. UL44 represents a hybrid processivity factor as it binds DNA directly like UL42, but forms a C clamp that may surround DNA like PCNA.
The cytomegalovirus DNA polymerase subunit UL44 forms a C clamp-shaped dimer.,Appleton BA, Loregian A, Filman DJ, Coen DM, Hogle JM Mol Cell. 2004 Jul 23;15(2):233-44. PMID:15260974<ref>PMID:15260974</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1t6l" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hcmv]]
[[Category: Human betaherpesvirus 5]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Appleton, B A]]
[[Category: Appleton BA]]
[[Category: Coen, D M]]
[[Category: Coen DM]]
[[Category: Filman, D J]]
[[Category: Filman DJ]]
[[Category: Hogle, J M]]
[[Category: Hogle JM]]
[[Category: Loregian, A]]
[[Category: Loregian A]]
[[Category: Processivity fold]]
[[Category: Replication]]
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