2e9x

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==Overview==
==Overview==
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The eukaryotic GINS complex is essential for the establishment of DNA, replication forks and replisome progression. We report the crystal, structure of the human GINS complex. The heterotetrameric complex adopts a, pseudo symmetrical layered structure comprising two heterodimers, creating, four subunit-subunit interfaces. The subunit structures of the, heterodimers consist of two alternating domains. The C-terminal domains of, the Sld5 and Psf1 subunits are connected by linker regions to the core, complex, and the C-terminal domain of Sld5 is important for core complex, assembly. In contrast, the C-terminal domain of Psf1 does not contribute, to the stability of the complex but is crucial for chromatin binding and, replication activity. These data suggest that the core complex ensures a, stable platform for the C-terminal domain of Psf1 to act as a key, interaction interface for other proteins in the replication-initiation, process.
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The eukaryotic GINS complex is essential for the establishment of DNA replication forks and replisome progression. We report the crystal structure of the human GINS complex. The heterotetrameric complex adopts a pseudo symmetrical layered structure comprising two heterodimers, creating four subunit-subunit interfaces. The subunit structures of the heterodimers consist of two alternating domains. The C-terminal domains of the Sld5 and Psf1 subunits are connected by linker regions to the core complex, and the C-terminal domain of Sld5 is important for core complex assembly. In contrast, the C-terminal domain of Psf1 does not contribute to the stability of the complex but is crucial for chromatin binding and replication activity. These data suggest that the core complex ensures a stable platform for the C-terminal domain of Psf1 to act as a key interaction interface for other proteins in the replication-initiation process.
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==Disease==
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Known diseases associated with this structure: Bare lymphocyte syndrome, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=170260 170260]], Bare lymphocyte syndrome, type I, due to TAP2 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=170261 170261]], Wegener-like granulomatosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=170261 170261]]
==About this Structure==
==About this Structure==
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[[Category: gins complex]]
[[Category: gins complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:14:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:07:49 2008''

Revision as of 15:07, 21 February 2008


2e9x, resolution 2.30Å

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The crystal structure of human GINS core complex

Contents

Overview

The eukaryotic GINS complex is essential for the establishment of DNA replication forks and replisome progression. We report the crystal structure of the human GINS complex. The heterotetrameric complex adopts a pseudo symmetrical layered structure comprising two heterodimers, creating four subunit-subunit interfaces. The subunit structures of the heterodimers consist of two alternating domains. The C-terminal domains of the Sld5 and Psf1 subunits are connected by linker regions to the core complex, and the C-terminal domain of Sld5 is important for core complex assembly. In contrast, the C-terminal domain of Psf1 does not contribute to the stability of the complex but is crucial for chromatin binding and replication activity. These data suggest that the core complex ensures a stable platform for the C-terminal domain of Psf1 to act as a key interaction interface for other proteins in the replication-initiation process.

Disease

Known diseases associated with this structure: Bare lymphocyte syndrome, type I OMIM:[170260], Bare lymphocyte syndrome, type I, due to TAP2 deficiency OMIM:[170261], Wegener-like granulomatosis OMIM:[170261]

About this Structure

2E9X is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the human GINS complex and its assembly and functional interface in replication initiation., Kamada K, Kubota Y, Arata T, Shindo Y, Hanaoka F, Nat Struct Mol Biol. 2007 May;14(5):388-96. Epub 2007 Apr 8. PMID:17417653

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