PDBsum entry 2ix2

Replication

PDB id: 2ix2

Contents

Protein chains

226 a.a. *

245 a.a. *

241 a.a. *

Waters ×120

* Residue conservation analysis

PDB id:

2ix2

Name:

Replication

Title:

Crystal structure of the heterotrimeric pcna from sulfolobus solfataricus

Structure:

DNA polymerase sliding clamp b. Chain: a. Synonym: proliferating cell nuclear antigen homolog b, pcna b. Engineered: yes. DNA polymerase sliding clamp c. Chain: b. Synonym: proliferating cell nuclear antigen homolog c, pcna c. Engineered: yes. DNA polymerase sliding clamp a.

Source:

Sulfolobus solfataricus. Organism_taxid: 2287. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Biol. unit:

Trimer (from PDB file)

Resolution:

2.20Å R-factor: 0.220 R-free: 0.273

Authors:

G.J.Williams,K.Johnson,S.A.Mcmahon,L.Carter,M.Oke,H.Liu,G.L.Taylor, M.F.White,J.H.Naismith

Key ref:

G.J.Williams et al. (2006). Structure of the heterotrimeric PCNA from Sulfolobus solfataricus. Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 944-948. PubMed id: 17012780 DOI: 10.1107/S1744309106034075

Date:

05-Jul-06 Release date: 04-Oct-06

Protein chain

P57766  (PCNA1_SULSO) -  DNA polymerase sliding clamp 1 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Seq: 249 a.a.

Struc: 226 a.a.

Protein chain

Q97Z84  (PCNA2_SULSO) -  DNA polymerase sliding clamp 2 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Seq: 245 a.a.

Struc: 245 a.a.

Protein chain

P57765  (PCNA3_SULSO) -  DNA polymerase sliding clamp 3 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Seq: 244 a.a.

Struc: 241 a.a.

DOI no: 10.1107/S1744309106034075

Acta Crystallogr Sect F Struct Biol Cryst Commun 62:944-948 (2006)

PubMed id: 17012780

Structure of the heterotrimeric PCNA from Sulfolobus solfataricus.

G.J.Williams, K.Johnson, J.Rudolf, S.A.McMahon, L.Carter, M.Oke, H.Liu, G.L.Taylor, M.F.White, J.H.Naismith.

ABSTRACT

PCNA is a ring-shaped protein that encircles DNA, providing a platform for the association of a wide variety of DNA-processing enzymes that utilize the PCNA sliding clamp to maintain proximity to their DNA substrates. PCNA is a homotrimer in eukaryotes, but a heterotrimer in crenarchaea such as Sulfolobus solfataricus. The three proteins are SsoPCNA1 (249 residues), SsoPCNA2 (245 residues) and SsoPCNA3 (259 residues). The heterotrimeric protein crystallizes in space group P2(1), with unit-cell parameters a = 44.8, b = 78.8, c = 125.6 A, beta = 100.5 degrees. The crystal structure of this heterotrimeric PCNA molecule has been solved using molecular replacement. The resulting structure to 2.3 A sheds light on the differential stabilities of the interactions observed between the three subunits and the specificity of individual subunits for partner proteins.

Selected figure(s)

Figure 3.
SsoPCNA3 is displaced from the ring relative to the observation for the huPCNA homotrimer (PDB code 1vym; Kontopidis et al., 2005[triangle]). The SsoPCNA trimer is coloured as in Fig. 2 [triangle] Figure 2-(a); the human trimer is coloured cyan, wheat and pale pink. The same displacement is seen when compared with the yeast homotrimer (Krishna et al., 1994[triangle]). The structures are shown in stereoview. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 October 1; 62(Pt 10): 944–948. Published online 2006 September 19. doi: 10.1107/S1744309106034075. Copyright [copyright] International Union of Crystallography 2006

Figure 4.
Stereoview of surface properties coloured by electrostatic potential of SsoPCNA. The orientation of the molecule is the same as in Fig. 2 [triangle] Figure 2-(a). 1 denotes the likely binding site for accessory proteins which bind to SsoPCNA1, 2 for SsoPCNA2 and 3 for SsoPCNA3. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 October 1; 62(Pt 10): 944–948. Published online 2006 September 19. doi: 10.1107/S1744309106034075. Copyright [copyright] International Union of Crystallography 2006

The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallogr Sect F Struct Biol Cryst Commun (2006, 62, 944-948) copyright 2006.

Figures were selected by an automated process.