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| {{STRUCTURE_2dla| PDB=2dla | SCENE= }} | | {{STRUCTURE_2dla| PDB=2dla | SCENE= }} |
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| '''Primase large subunit amino terminal domain from Pyrococcus horikoshii'''
| | ===Primase large subunit amino terminal domain from Pyrococcus horikoshii=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17286576}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17286576 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17286576}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Helix bundle]] | | [[Category: Helix bundle]] |
| [[Category: Twisted beta-sheet]] | | [[Category: Twisted beta-sheet]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:40:02 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:10:37 2008'' |
