2dla

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2dla" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:2dla.png|left|200px]]
+
==Primase large subunit amino terminal domain from Pyrococcus horikoshii==
 +
<StructureSection load='2dla' size='340' side='right' caption='[[2dla]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2dla]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii_ot3 Pyrococcus horikoshii ot3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DLA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DLA 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=2dla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dla OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dla RCSB], [http://www.ebi.ac.uk/pdbsum/2dla PDBsum]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Archaeal/eukaryotic primases form a heterodimer consisting of a small catalytic subunit (PriS) and a large subunit (PriL). The heterodimer complex synthesizes primer oligoribonucleotides that are required for chromosomal replication. Here, we describe crystallographic and biochemical studies of the N-terminal domain (NTD) of PriL (PriL(NTD); residues 1-222) that bind to PriS from a hyperthermophilic archaeon, Pyrococcus horikoshii, at 2.9 A resolution. The PriL(NTD) structure consists of two subdomains, the helix-bundle and twisted-strand domains. The latter is structurally flexible, and is expected to contain a PriS interaction site. Pull-down and surface plasmon resonance analyses of structure-based deletion and alanine scanning mutants showed that the conserved hydrophobic Tyr155-Tyr156-Ile157 region near the flexible region is the PriS-binding site, as the Y155A/Y156A/I157A mutation markedly reduces PriS binding, by 1000-fold. These findings and a structural comparison with a previously reported PriL(NTD)-PriS complex suggest that the presented alternative conformations of the twisted-strand domain facilitate the heterodimer assembly.
-
{{STRUCTURE_2dla| PDB=2dla | SCENE= }}
+
Molecular basis for the subunit assembly of the primase from an archaeon Pyrococcus horikoshii.,Ito N, Matsui I, Matsui E FEBS J. 2007 Mar;274(5):1340-51. Epub 2007 Feb 5. PMID:17286576<ref>PMID:17286576</ref>
-
===Primase large subunit amino terminal domain from Pyrococcus horikoshii===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_17286576}}
+
== References ==
-
 
+
<references/>
-
==About this Structure==
+
__TOC__
-
[[2dla]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii_ot3 Pyrococcus horikoshii ot3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DLA OCA].
+
</StructureSection>
[[Category: Pyrococcus horikoshii ot3]]
[[Category: Pyrococcus horikoshii ot3]]
[[Category: Ito, N.]]
[[Category: Ito, N.]]

Revision as of 15:26, 12 October 2014

Primase large subunit amino terminal domain from Pyrococcus horikoshii

2dla, resolution 2.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dla"
Personal tools