2q9q
From Proteopedia
(Difference between revisions)
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<StructureSection load='2q9q' size='340' side='right'caption='[[2q9q]], [[Resolution|resolution]] 2.36Å' scene=''> | <StructureSection load='2q9q' size='340' side='right'caption='[[2q9q]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2q9q]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2q9q]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q9Q FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.36Å</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q9q OCA], [https://pdbe.org/2q9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q9q RCSB], [https://www.ebi.ac.uk/pdbsum/2q9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q9q ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q9q OCA], [https://pdbe.org/2q9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q9q RCSB], [https://www.ebi.ac.uk/pdbsum/2q9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q9q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PSF2_HUMAN PSF2_HUMAN] The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA.<ref>PMID:17417653</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2q9q ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2q9q ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The GINS complex, which contains the four subunits Sld5, Psf1, Psf2, and Psf3, is essential for both the initiation and progression of DNA replication in eukaryotes. GINS associates with the MCM2-7 complex and Cdc45 to activate the eukaryotic minichromosome maintenance helicase. It also appears to interact with and stimulate the polymerase activities of DNA polymerase epsilon and the DNA polymerase alpha-primase complex. To further understand the functional role of GINS, we determined the crystal structure of the full-length human GINS heterotetramer. Each of the four subunits has a major domain composed of an alpha-helical bundle-like structure. With the exception of Psf1, each of the other subunits has a small domain containing a three-stranded beta-sheet core. Each full-length protein in the crystal has unstructured regions that are all located on the surface of GINS and are probably involved in its interaction with other replication factors. The four subunits contact each other mainly through alpha-helices to form a ring-like tetramer with a central pore. This pore is partially plugged by a 16-residue peptide from the Psf3 N terminus, which is unique to some eukaryotic Psf3 proteins and is not required for tetramer formation. Removal of these N-terminal 16 residues of Psf3 from the GINS tetramer increases the opening of the pore by 80%, suggesting a mechanism by which accessibility to the pore may be regulated. The structural data presented here indicate that the GINS tetramer is a highly stable complex with multiple flexible surface regions. | ||
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| - | Crystal structure of the GINS complex and functional insights into its role in DNA replication.,Chang YP, Wang G, Bermudez V, Hurwitz J, Chen XS Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12685-90. Epub 2007 Jul 25. PMID:17652513<ref>PMID:17652513</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2q9q" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chang | + | [[Category: Chang YP]] |
| - | [[Category: Chen | + | [[Category: Chen XS]] |
| - | [[Category: Wang | + | [[Category: Wang G]] |
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Current revision
The crystal structure of full length human GINS complex
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