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| | <StructureSection load='3ifv' size='340' side='right'caption='[[3ifv]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3ifv' size='340' side='right'caption='[[3ifv]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ifv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_29605 Atcc 29605]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IFV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ifv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_volcanii Haloferax volcanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IFV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcna ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2246 ATCC 29605])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ifv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ifv OCA], [https://pdbe.org/3ifv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ifv RCSB], [https://www.ebi.ac.uk/pdbsum/3ifv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ifv ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ifv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ifv OCA], [https://pdbe.org/3ifv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ifv RCSB], [https://www.ebi.ac.uk/pdbsum/3ifv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ifv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/D0VWY8_HALVO D0VWY8_HALVO]] Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication (By similarity).[HAMAP-Rule:MF_00317]
| + | [https://www.uniprot.org/uniprot/D0VWY8_HALVO D0VWY8_HALVO] Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication (By similarity).[HAMAP-Rule:MF_00317] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 29605]] | + | [[Category: Haloferax volcanii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bunting, K A]] | + | [[Category: Bunting KA]] |
| - | [[Category: Christofi, P]] | + | [[Category: Christofi P]] |
| - | [[Category: Morroll, S]] | + | [[Category: Morroll S]] |
| - | [[Category: Winter, J A]] | + | [[Category: Winter JA]] |
| - | [[Category: Halophilic]]
| + | |
| - | [[Category: Processivity factor]]
| + | |
| - | [[Category: Replication]]
| + | |
| - | [[Category: Sliding clamp]]
| + | |
| Structural highlights
Function
D0VWY8_HALVO Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication (By similarity).[HAMAP-Rule:MF_00317]
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
BACKGROUND: The high intracellular salt concentration required to maintain a halophilic lifestyle poses challenges to haloarchaeal proteins that must stay soluble, stable and functional in this extreme environment. Proliferating cell nuclear antigen (PCNA) is a fundamental protein involved in maintaining genome integrity, with roles in both DNA replication and repair. To investigate the halophilic adaptation of such a key protein we have crystallised and solved the structure of Haloferax volcanii PCNA (HvPCNA) to a resolution of 2.0 A. RESULTS: The overall architecture of HvPCNA is very similar to other known PCNAs, which are highly structurally conserved. Three commonly observed adaptations in halophilic proteins are higher surface acidity, bound ions and increased numbers of intermolecular ion pairs (in oligomeric proteins). HvPCNA possesses the former two adaptations but not the latter, despite functioning as a homotrimer. Strikingly, the positive surface charge considered key to PCNA's role as a sliding clamp is dramatically reduced in the halophilic protein. Instead, bound cations within the solvation shell of HvPCNA may permit sliding along negatively charged DNA by reducing electrostatic repulsion effects. CONCLUSION: The extent to which individual proteins adapt to halophilic conditions varies, presumably due to their diverse characteristics and roles within the cell. The number of ion pairs observed in the HvPCNA monomer-monomer interface was unexpectedly low. This may reflect the fact that the trimer is intrinsically stable over a wide range of salt concentrations and therefore additional modifications for trimer maintenance in high salt conditions are not required. Halophilic proteins frequently bind anions and cations and in HvPCNA cation binding may compensate for the remarkable reduction in positive charge in the pore region, to facilitate functional interactions with DNA. In this way, HvPCNA may harness its environment as opposed to simply surviving in extreme halophilic conditions.
The crystal structure of Haloferax volcanii proliferating cell nuclear antigen reveals unique surface charge characteristics due to halophilic adaptation.,Winter JA, Christofi P, Morroll S, Bunting KA BMC Struct Biol. 2009 Aug 22;9:55. PMID:19698123[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Winter JA, Christofi P, Morroll S, Bunting KA. The crystal structure of Haloferax volcanii proliferating cell nuclear antigen reveals unique surface charge characteristics due to halophilic adaptation. BMC Struct Biol. 2009 Aug 22;9:55. PMID:19698123 doi:10.1186/1472-6807-9-55
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