1g71: Difference between revisions

Revision as of 04:48, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1g71.png

Template:STRUCTURE 1g71

CRYSTAL STRUCTURE OF PYROCOCCUS FURIOSUS DNA PRIMASECRYSTAL STRUCTURE OF PYROCOCCUS FURIOSUS DNA PRIMASE

Template:ABSTRACT PUBMED 11135672

About this StructureAbout this Structure

1G71 is a Single protein structure of sequence from Pyrococcus furiosus. 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 Jul 1 04:48:21 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1g71.gif|left|200px]]
+{{Seed}}
+[[Image:1g71.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1g71|  PDB=1g71  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF PYROCOCCUS FURIOSUS DNA PRIMASE'''
+===CRYSTAL STRUCTURE OF PYROCOCCUS FURIOSUS DNA PRIMASE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11135672}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11135672 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11135672}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Kaiser, J T.]]
 [[Category: Zinc-knuckle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:13:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 04:48:21 2008''