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==NMR structure of the C-terminal domain of pUL89==
==NMR structure of the C-terminal domain of pUL89==
<StructureSection load='2kn8' size='340' side='right'caption='[[2kn8]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='2kn8' size='340' side='right'caption='[[2kn8]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2kn8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KN8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2kn8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KN8 FirstGlance]. <br>
</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=2kn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kn8 OCA], [https://pdbe.org/2kn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kn8 RCSB], [https://www.ebi.ac.uk/pdbsum/2kn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kn8 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kn8 OCA], [https://pdbe.org/2kn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kn8 RCSB], [https://www.ebi.ac.uk/pdbsum/2kn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kn8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6RXE9_HCMV Q6RXE9_HCMV]
== 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=2kn8 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=2kn8 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In a previous study, we identified 12 conserved domains within pUL89, the small terminase subunit of the human cytomegalovirus. A latter study showed that the fragment pUL89(580-600) plays an important role in the formation of the terminase complex by interacting with the large terminase subunit pUL56. In this study, analysis was performed to solve the structure of pUL89(568-635) in 50% H2O/50% acetonitrile (v/v). We showed that pUL89(568-635) consists of four alpha helices, but we did not identify any tertiary structure. The fragment 580-600 formed an amphipathic alpha helix, which had a hydrophobic side highly conserved among herpesviral homologs of pUL89; this was not observed for its hydrophilic side. The modeling of pUL89(457-612) using the recognition fold method allowed us to position pUL89(580-600) within this domain. The theoretical structure highlighted three important features. First, we identified a metal-binding pocket containing residues Asp(463), Glu(534), and Glu(588), which are highly conserved among pUL89 homologs. Second, the model predicted a positively charged surface able to interact with the DNA duplex during the nicking event. Third, a hydrophobic patch on the top of the catalytic site suggested that this may constitute part of the pUL89 site recognized by pUL56 potentially involved in DNA binding.
Insight into the structure of the pUL89 C-terminal domain of the human cytomegalovirus terminase complex.,Couvreux A, Hantz S, Marquant R, Champier G, Alain S, Morellet N, Bouaziz S Proteins. 2010 May 1;78(6):1520-30. PMID:20099308<ref>PMID:20099308</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kn8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Alain, S]]
[[Category: Alain S]]
[[Category: Bouaziz, S]]
[[Category: Bouaziz S]]
[[Category: Champier, G]]
[[Category: Champier G]]
[[Category: Couvreux, A]]
[[Category: Couvreux A]]
[[Category: Hantz, S]]
[[Category: Hantz S]]
[[Category: Marquant, R]]
[[Category: Marquant R]]
[[Category: Morellet, N]]
[[Category: Morellet N]]
[[Category: Dna binding protein]]
[[Category: Nhcmv]]
[[Category: Protein binding]]
[[Category: Pul89]]
[[Category: Terminase]]

Latest revision as of 06:46, 1 May 2024

NMR structure of the C-terminal domain of pUL89

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