5vbn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of human DNA polymerase epsilon B-subunit in complex with C-terminal domain of catalytic subunit== | |
| + | <StructureSection load='5vbn' size='340' side='right' caption='[[5vbn]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5vbn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VBN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vbn OCA], [http://pdbe.org/5vbn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vbn RCSB], [http://www.ebi.ac.uk/pdbsum/5vbn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vbn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/DPOE1_HUMAN DPOE1_HUMAN]] Facial dysmorphism - immunodeficiency - livedo - short stature. Disease susceptibility is associated with variations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DPOE2_HUMAN DPOE2_HUMAN]] Participates in DNA repair and in chromosomal DNA replication. [[http://www.uniprot.org/uniprot/DPOE1_HUMAN DPOE1_HUMAN]] Participates in DNA repair and in chromosomal DNA replication. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The eukaryotic B-family DNA polymerases include four members, Polalpha, Poldelta, Pol, and Polzeta, which share common architectural features, such as the exonuclease/polymerase and C-terminal domains (CTDs) of catalytic subunits bound to indispensable B-subunits, which serve as scaffolds that mediate interactions with other components of the replication machinery. Crystal structures for the B-subunits of Polalpha and Poldelta/Polzeta have been reported; the former within the primosome and separately with CTD, and the latter with the N-terminal domain (NTD) of the C-subunit. Here we present the crystal structure of the human Pol B-subunit (p59) in complex with CTD of the catalytic subunit (p261C). The structure revealed a well-defined electron density for p261C and the phosphodiesterase (PDE) and oligonucleotide/oligosaccharide-binding domains of p59. However, electron density was missing for the p59 NTD and for the linker connecting it to the PDE domain. Similar to Polalpha, p261C contains a three-helix bundle in the middle and zinc-binding modules (Zn1 and Zn2) on each side. Intersubunit interactions involving 11 hydrogen bonds and numerous hydrophobic contacts account for stable complex formation with a buried surface area of 3094 A2 Comparative structural analysis of p59-p261C with the corresponding Polalpha complex revealed significant differences between the B-subunits and CTDs as well as their interaction interfaces. The B-subunit of Poldelta/Polzeta also substantially differs from B-subunits of either Polalpha or Pol. This work provides a structural basis to explain biochemical and genetic data on the importance of B-subunit integrity in replisome function in vivo. | ||
| - | + | Crystal structure of the human Pol B-subunit in complex with the C-terminal domain of the catalytic subunit.,Baranovskiy AG, Gu J, Babayeva ND, Kurinov I, Pavlov YI, Tahirov TH J Biol Chem. 2017 Jul 26. pii: jbc.M117.792705. doi: 10.1074/jbc.M117.792705. PMID:28747437<ref>PMID:28747437</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5vbn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: DNA-directed DNA polymerase]] | ||
| + | [[Category: Babayeva, N D]] | ||
| + | [[Category: Baranovskiy, A G]] | ||
| + | [[Category: Gu, J]] | ||
| + | [[Category: Suwa, Y]] | ||
| + | [[Category: Tahirov, T H]] | ||
| + | [[Category: B-subunit]] | ||
| + | [[Category: Catalytic subunit]] | ||
| + | [[Category: Dna polymerase]] | ||
| + | [[Category: Dna polymerase epsilon]] | ||
| + | [[Category: Dna replication]] | ||
| + | [[Category: Polymerase]] | ||
| + | [[Category: Replication]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 09:09, 9 August 2017
Crystal Structure of human DNA polymerase epsilon B-subunit in complex with C-terminal domain of catalytic subunit
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