2dla

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(New page: 200px<br /><applet load="2dla" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dla, resolution 2.9&Aring;" /> '''Primase large subunit...)
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[[Image:2dla.gif|left|200px]]<br /><applet load="2dla" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2dla, resolution 2.9&Aring;" />
caption="2dla, resolution 2.9&Aring;" />
'''Primase large subunit amino terminal domain from Pyrococcus horikoshii'''<br />
'''Primase large subunit amino terminal domain from Pyrococcus horikoshii'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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2DLA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DLA OCA].
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2DLA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DLA OCA].
==Reference==
==Reference==
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[[Category: twisted beta-sheet]]
[[Category: twisted beta-sheet]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:39:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:59:55 2008''

Revision as of 15:00, 21 February 2008

Image:2dla.gif

2dla, resolution 2.9Å

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Primase large subunit amino terminal domain from Pyrococcus horikoshii

Overview

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.

About this Structure

2DLA is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

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

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