This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1v34

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 1v34 |SIZE=350|CAPTION= <scene name='initialview01'>1v34</scene>, resolution 2.7&Aring;
|PDB= 1v34 |SIZE=350|CAPTION= <scene name='initialview01'>1v34</scene>, resolution 2.7&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=UTP:URIDINE 5'-TRIPHOSPHATE'>UTP</scene>
+
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=UTP:URIDINE 5&#39;-TRIPHOSPHATE'>UTP</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
Line 35: Line 35:
[[Category: structural genomic]]
[[Category: structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:40:16 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:57:03 2008''

Revision as of 11:57, 23 March 2008


PDB ID 1v34

Drag the structure with the mouse to rotate
, resolution 2.7Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Pyrococcus horikoshii DNA primase-UTP complex


Overview

BACKGROUND: In chromosomal DNA replication, DNA primase initiates the synthesis of a dinucleotide on a single-stranded template DNA, and elongates it to form a primer RNA for the replicative DNA polymerase. Although the apo-structure of an archaeal primase has been reported, the mechanism of primer synthesis by the eukaryotic-type primase still remains to be elucidated. RESULTS: In this study, we present the crystal structure of the eukaryotic-type DNA primase from the hyperthermophilic archaeon (Pyrococcus horikoshii) with the uridine 5'-triphosphate (UTP). In the present primase-UTP complex, the primase binds the triphosphate moiety of the UTP at the active site, which includes Asp95, Asp97, and Asp280, the essential residues for the nucleotidyl transfer reaction. CONCLUSION: The nucleotide binding geometry in this complex explains the previous biochemical analyses of the eukaryotic primase. Based on the complex structure, we constructed a model between the DNA primase and a primer/template DNA for the primer synthesis. This model facilitates the comprehension of the reported features of DNA primase.

About this Structure

1V34 is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex: implications for the mechanism of primer synthesis., Ito N, Nureki O, Shirouzu M, Yokoyama S, Hanaoka F, Genes Cells. 2003 Dec;8(12):913-23. PMID:14750947

Page seeded by OCA on Sun Mar 23 13:57:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools