5vbn

<StructureSection load='5vbn' size='340' side='right' caption='[[5vbn]], [[Resolution|resolution]] 2.35&Aring;' scene=''>

<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>

== 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.

[[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.

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.

 

== References ==

[[Category: DNA-directed DNA polymerase]]

[[Category: Babayeva, N D]]

[[Category: Baranovskiy, A G]]

[[Category: Gu, J]]

[[Category: Suwa, Y]]

[[Category: Tahirov, T H]]

[[Category: Transferase]]