1g71

Revision as of 16:39, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1g71" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g71, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)

CRYSTAL STRUCTURE OF PYROCOCCUS FURIOSUS DNA PRIMASE

File:1g71.gif


1g71, resolution 2.3Å

Drag the structure with the mouse to rotate

OverviewOverview

Primases are essential components of the DNA replication apparatus in, every organism. They catalyze the synthesis of oligoribonucleotides on, single-stranded DNA, which subsequently serve as primers for the, replicative DNA polymerases. In contrast to bacterial primases, the, archaeal enzymes are closely related to their eukaryotic counterparts. We, have solved the crystal structure of the catalytic primase subunit from, the hyperthermophilic archaeon Pyrococcus furiosus at 2.3 A resolution by, multiwavelength anomalous dispersion methods. The structure shows a, two-domain arrangement with a novel zinc knuckle motif located in the, primase (prim) domain. In this first structure of a complete protein of, the archaeal/eukaryotic primase family, the arrangement of the, catalytically active residues resembles the active sites of various DNA, polymerases that are unrelated in fold.

About this StructureAbout this Structure

1G71 is a Single protein structure of sequence from Pyrococcus furiosus with ZN, CL and SO4 as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a DNA-dependent RNA polymerase (DNA primase)., Augustin MA, Huber R, Kaiser JT, Nat Struct Biol. 2001 Jan;8(1):57-61. PMID:11135672

Page seeded by OCA on Tue Nov 20 15:46:15 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA