1b8h
From Proteopedia
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| - | [[Image:1b8h.gif|left|200px]]<br /><applet load="1b8h" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1b8h, resolution 3.00Å" /> | ||
| - | '''SLIDING CLAMP, DNA POLYMERASE'''<br /> | ||
| - | == | + | ==SLIDING CLAMP, DNA POLYMERASE== |
| + | <StructureSection load='1b8h' size='340' side='right'caption='[[1b8h]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1b8h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB69 Escherichia phage RB69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B8H FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=1b8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8h OCA], [https://pdbe.org/1b8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b8h RCSB], [https://www.ebi.ac.uk/pdbsum/1b8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b8h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CLAMP_BPR69 CLAMP_BPR69] Sliding clamp that encircles the genomic DNA and links the DNA polymerase to the template to control the processivity of DNA synthesis. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. Interaction with the sliding-clamp-loader opens the sliding clamp so that it can be loaded around the DNA template. During transcription, encircles the DNA and tethers host RNA polymerase (RNAP) to it.[HAMAP-Rule:MF_04161] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b8/1b8h_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1b8h ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
We have solved the crystal structures of the bacteriophage RB69 sliding clamp, its complex with a peptide essential for DNA polymerase interactions, and the DNA polymerase complexed with primer-template DNA. The editing complex structure shows a partially melted duplex DNA exiting from the exonuclease domain at an unexpected angle and significant changes in the protein structure. The clamp complex shows the C-terminal 11 residues of polymerase bound in a hydrophobic pocket, and it allows docking of the editing and clamp structures together. The peptide binds to the sliding clamp at a position identical to that of a replication inhibitor peptide bound to PCNA, suggesting that the replication inhibitor protein p21CIP1 functions by competing with eukaryotic polymerases for the same binding pocket on the clamp. | We have solved the crystal structures of the bacteriophage RB69 sliding clamp, its complex with a peptide essential for DNA polymerase interactions, and the DNA polymerase complexed with primer-template DNA. The editing complex structure shows a partially melted duplex DNA exiting from the exonuclease domain at an unexpected angle and significant changes in the protein structure. The clamp complex shows the C-terminal 11 residues of polymerase bound in a hydrophobic pocket, and it allows docking of the editing and clamp structures together. The peptide binds to the sliding clamp at a position identical to that of a replication inhibitor peptide bound to PCNA, suggesting that the replication inhibitor protein p21CIP1 functions by competing with eukaryotic polymerases for the same binding pocket on the clamp. | ||
| - | + | Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex.,Shamoo Y, Steitz TA Cell. 1999 Oct 15;99(2):155-66. PMID:10535734<ref>PMID:10535734</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1b8h" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Shamoo | + | <references/> |
| - | [[Category: Steitz | + | __TOC__ |
| - | + | </StructureSection> | |
| - | + | [[Category: Escherichia phage RB69]] | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Shamoo Y]] | |
| - | + | [[Category: Steitz TA]] | |
| - | + | ||
Current revision
SLIDING CLAMP, DNA POLYMERASE
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