1quq
From Proteopedia
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| - | [[Image:1quq.gif|left|200px]] | + | [[Image:1quq.gif|left|200px]] |
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| - | '''COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32''' | + | {{Structure |
| + | |PDB= 1quq |SIZE=350|CAPTION= <scene name='initialview01'>1quq</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QUQ is a [ | + | 1QUQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUQ OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding., Bochkarev A, Bochkareva E, Frappier L, Edwards AM, EMBO J. 1999 Aug 16;18(16):4498-504. PMID:[http:// | + | The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding., Bochkarev A, Bochkareva E, Frappier L, Edwards AM, EMBO J. 1999 Aug 16;18(16):4498-504. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10449415 10449415] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ssdna-binding]] | [[Category: ssdna-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:43:00 2008'' |
Revision as of 11:43, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32
Overview
Replication protein A (RPA), the eukaryote single-stranded DNA-binding protein (SSB), is a heterotrimer. The largest subunit, RPA70, which harbours the major DNA-binding activity, has two DNA-binding domains that each adopt an OB-fold. The complex of the two smaller subunits, RPA32 and RPA14, has weak DNA-binding activity but the mechanism of DNA binding is unknown. We have determined the crystal structure of the proteolytic core of RPA32 and RPA14, which consists of the central two-thirds of RPA32 and the entire RPA14 subunit. The structure revealed that RPA14 and the central part of RPA32 are structural homologues. Each subunit contains a central OB-fold domain, which also resembles the DNA-binding domains in RPA70; an N-terminal extension that interacts with the central OB-fold domain; and a C-terminal helix that mediate heterodimerization via a helix-helix interaction. The OB-fold of RPA32, but not RPA14, possesses additional similarity to the RPA70 DNA-binding domains, supporting a DNA-binding role for RPA32. The discovery of a third and fourth OB-fold in RPA suggests that the quaternary structure of SSBs, which in Bacteria and Archaea are also tetramers of OB-folds, is conserved in evolution. The structure also suggests a mechanism for RPA trimer formation.
About this Structure
1QUQ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding., Bochkarev A, Bochkareva E, Frappier L, Edwards AM, EMBO J. 1999 Aug 16;18(16):4498-504. PMID:10449415
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