6a9w

<table><tr><td colspan='2'>[[6a9w]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A9W FirstGlance]. <br>

</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=6a9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9w OCA], [http://pdbe.org/6a9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a9w RCSB], [http://www.ebi.ac.uk/pdbsum/6a9w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9w ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

A novel DNA polymerase found in the deep-sea vent phage NrS-1, was confirmed to have both DNA polymerase and primase activities. In this polymerase, the N-terminal residues 1-300 (referred to as N300) are the core region required for polymerizing DNA and catalyzing de novo DNA synthesis. Here, the crystal structure of N300 was solved at a resolution of 1.80A. The overall structure consists of a prim/pol domain and a helix bundle domain, which are separated by a 14-residue-long flexible tether (residues 177-190). Both the prim/pol domain of N300 and other primase-polymerases (prim-pol) encompass an analogous fold with conserved catalytic residues. Mutagenesis and enzymatic activity assays show that the acidic active-site residue E139 is required for both polymerase and primase activities. Functional assays confirm the essentiality of the helix bundle domain for primase activity. Furthermore, we identified a mutant (N300-Y261A) of the helix bundle domain, which probably plays an indispensable role in the primer initiation and recognition of template DNA.

 

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== References ==

[[Category: Guo, H J]]

[[Category: He, J H]]

[[Category: Li, M J]]

[[Category: Liu, X P]]

[[Category: Wang, T L]]

[[Category: Wu, H]]

[[Category: Xu, C Y]]

[[Category: Yu, F]]

[[Category: Zhou, H]]

[[Category: Replication]]