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| | ==Crystal Structure of the Pyrococcus furiosus SMC Protein Hinge Domain== | | ==Crystal Structure of the Pyrococcus furiosus SMC Protein Hinge Domain== |
| - | <StructureSection load='3nwc' size='340' side='right' caption='[[3nwc]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3nwc' size='340' side='right'caption='[[3nwc]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nwc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NWC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nwc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NWC FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.6961Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3nwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nwc RCSB], [http://www.ebi.ac.uk/pdbsum/3nwc PDBsum]</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=3nwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nwc OCA], [https://pdbe.org/3nwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nwc RCSB], [https://www.ebi.ac.uk/pdbsum/3nwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nwc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3nwc" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Pyrococcus furiosus]] | | [[Category: Pyrococcus furiosus]] |
| - | [[Category: Griese, J J]] | + | [[Category: Griese JJ]] |
| - | [[Category: Hopfner, K P]] | + | [[Category: Hopfner KP]] |
| - | [[Category: Cell cycle]]
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| - | [[Category: Dimerization]]
| + | |
| - | [[Category: Dna binding]]
| + | |
| - | [[Category: Smc hinge domain]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Structural Maintenance of Chromosomes (SMC) proteins are essential for a wide range of processes including chromosome structure and dynamics, gene regulation, and DNA repair. While bacteria and archaea have one SMC protein that forms a homodimer, eukaryotes possess three distinct SMC complexes, consisting of heterodimeric pairs of six different SMC proteins. SMC holocomplexes additionally contain several specific regulatory subunits. The bacterial SMC complex is required for chromosome condensation and segregation. In eukaryotes, this function is carried out by the condensin (SMC2-SMC4) complex. SMC proteins consist of N-terminal and C-terminal domains that fold back onto each other to create an ATPase "head" domain, connected to a central "hinge" domain via a long coiled-coil region. The hinge domain mediates dimerization of SMC proteins and binds DNA. This activity implicates a direct involvement of the hinge domain in the action of SMC proteins on DNA. We studied the SMC hinge domain from the thermophilic archaeon Pyrococcus furiosus. Its crystal structure shows that the SMC hinge domain fold is largely conserved between archaea and bacteria as well as eukarya. Like the eukaryotic condensin hinge domain, the P. furiosus SMC hinge domain preferentially binds single-stranded DNA (ssDNA), but its affinity for DNA is weaker than that of its eukaryotic counterpart, and point mutations reveal that its DNA-binding surface is more confined. The ssDNA-binding activity of its hinge domain might play a role in the DNA-loading process of the prokaryotic SMC complex during replication. Proteins 2011. (c) 2010 Wiley-Liss, Inc.
Structure and DNA-binding activity of the Pyrococcus furiosus SMC protein hinge domain.,Griese JJ, Hopfner KP Proteins. 2011 Feb;79(2):558-68. PMID:21117236[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Griese JJ, Hopfner KP. Structure and DNA-binding activity of the Pyrococcus furiosus SMC protein hinge domain. Proteins. 2011 Feb;79(2):558-68. PMID:21117236 doi:10.1002/prot.22903
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