1quq
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1quq.gif|left|200px]] | [[Image:1quq.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1quq", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_1quq| PDB=1quq | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32''' | '''COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32''' | ||
| Line 29: | Line 26: | ||
[[Category: Edwards, A M.]] | [[Category: Edwards, A M.]] | ||
[[Category: Frappier, L.]] | [[Category: Frappier, L.]] | ||
| - | [[Category: | + | [[Category: Ob-fold]] |
| - | [[Category: | + | [[Category: Rpa]] |
| - | [[Category: | + | [[Category: Ssdna-binding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:43:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:43, 3 May 2008
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 Page seeded by OCA on Sat May 3 06:43:41 2008
