2nti

From Proteopedia

(Difference between revisions)

Revision as of 17:36, 15 August 2018

Crystal structure of PCNA123 heterotrimer.

Structural highlights

2nti is a 9 chain structure with sequence from Sulso. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	2ixj, 2izo, 2ix2, 2io4
Gene:	pcnB, pcnA-2 (SULSO), pcnC, pcnA-2 (SULSO), pcnA, pcnA-1 (SULSO)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PCNA2_SULSO] Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. [PCNA1_SULSO] Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. [PCNA3_SULSO] Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

DNA sliding clamps form an oligomeric ring encircling DNA and serve as a moving platform for DNA-processing proteins. The opening and closing of a sliding-clamp ring is essential to load the clamp onto DNA in order to perform its functions. The molecular details of how clamp rings open and enclose DNA are still not clear. Three PCNA homologues have been found in Sulfolobus solfataricus which form a heterotrimer. Taking advantage of their hetero-oligomeric nature, the structures of the PCNAs in monomeric PCNA3, dimeric PCNA1-PCNA2 and trimeric PCNA1-PCNA2-PCNA3 forms were determined at resolutions of 2.6-1.9 A. The distinct oligomeric structures represent different stages in ring formation, which were verified in solution by ultracentrifugation analysis. The heterodimer opens in a V-shape of 130 degrees , while the heterotrimers form a ring with a 120 degrees rotation between monomers. The association of a rigid PCNA3 monomer with an opened PCNA1-PCNA2 heterodimer closes the ring and introduces a spring tension in the PCNA1-PCNA2 interface, thus bending the nine-stranded intermolecular beta-sheet to fit the 120 degrees rotation. The release of the spring tension as PCNA3 dissociates from the ring may facilitate ring opening. The structural features in different assemblies present a molecular model for clamp ring assembly and opening.

Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and opening.,Hlinkova V, Xing G, Bauer J, Shin YJ, Dionne I, Rajashankar KR, Bell SD, Ling H Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):941-9. Epub 2008, Aug 13. PMID:18703842^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hlinkova V, Xing G, Bauer J, Shin YJ, Dionne I, Rajashankar KR, Bell SD, Ling H. Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and opening. Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):941-9. Epub 2008, Aug 13. PMID:18703842 doi:10.1107/S0907444908021665

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nti"

@@ Line 1: / Line 1: @@
 ==Crystal structure of PCNA123 heterotrimer.==
 <StructureSection load='2nti' size='340' side='right' caption='[[2nti]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ixj|2ixj]], [[2izo|2izo]], [[2ix2|2ix2]], [[2io4|2io4]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcnB, pcnA-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO]), pcnC, pcnA-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO]), pcnA, pcnA-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nti OCA], [http://pdbe.org/2nti PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nti RCSB], [http://www.ebi.ac.uk/pdbsum/2nti PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nti OCA], [http://pdbe.org/2nti PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nti RCSB], [http://www.ebi.ac.uk/pdbsum/2nti PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nti ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/2nti_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/2nti_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2nti

From Proteopedia

Revision as of 17:36, 15 August 2018

Crystal structure of PCNA123 heterotrimer.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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