1quq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1quq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1quq OCA], [http://www.ebi.ac.uk/pdbsum/1quq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1quq RCSB]</span>
}}
}}
Line 30: Line 33:
[[Category: ssdna-binding]]
[[Category: ssdna-binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:43:00 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:19:16 2008''

Revision as of 20:19, 30 March 2008


PDB ID 1quq

Drag the structure with the mouse to rotate
, resolution 2.5Å
Resources: FirstGlance, OCA, PDBsum, RCSB
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

Page seeded by OCA on Sun Mar 30 23:19:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools