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[[Image:1unn.gif|left|200px]]


{{Structure
==Complex of beta-clamp processivity factor and little finger domain of PolIV==
|PDB= 1unn |SIZE=350|CAPTION= <scene name='initialview01'>1unn</scene>, resolution 1.90&Aring;
<StructureSection load='1unn' size='340' side='right'caption='[[1unn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+D'>AC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1unn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UNN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UNN FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1unn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1unn OCA], [https://pdbe.org/1unn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1unn RCSB], [https://www.ebi.ac.uk/pdbsum/1unn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1unn ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1unn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1unn OCA], [http://www.ebi.ac.uk/pdbsum/1unn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1unn RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/DPO3B_ECOLI DPO3B_ECOLI] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA.
== 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/un/1unn_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=1unn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Y-family DNA polymerases can extend primer strands across template strand lesions that stall replicative polymerases. The poor processivity and fidelity of these enzymes, key to their biological role, requires that their access to the primer-template junction is both facilitated and regulated in order to minimize mutations. These features are believed to be provided by interaction with processivity factors, beta-clamp or proliferating cell nuclear antigen (PCNA), which are also essential for the function of replicative DNA polymerases. The basis for this interaction is revealed by the crystal structure of the complex between the 'little finger' domain of the Y-family DNA polymerase Pol IV and the beta-clamp processivity factor, both from Escherichia coli. The main interaction involves a C-terminal peptide of Pol IV, and is similar to interactions seen between isolated peptides and other processivity factors. However, this first structure of an entire domain of a binding partner with an assembled clamp reveals a substantial secondary interface, which maintains the polymerase in an inactive orientation, and may regulate the switch between replicative and Y-family DNA polymerases in response to a template strand lesion.


'''COMPLEX OF BETA-CLAMP PROCESSIVITY FACTOR AND LITTLE FINGER DOMAIN OF POLIV'''
Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp.,Bunting KA, Roe SM, Pearl LH EMBO J. 2003 Nov 3;22(21):5883-92. PMID:14592985<ref>PMID:14592985</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1unn" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Y-family DNA polymerases can extend primer strands across template strand lesions that stall replicative polymerases. The poor processivity and fidelity of these enzymes, key to their biological role, requires that their access to the primer-template junction is both facilitated and regulated in order to minimize mutations. These features are believed to be provided by interaction with processivity factors, beta-clamp or proliferating cell nuclear antigen (PCNA), which are also essential for the function of replicative DNA polymerases. The basis for this interaction is revealed by the crystal structure of the complex between the 'little finger' domain of the Y-family DNA polymerase Pol IV and the beta-clamp processivity factor, both from Escherichia coli. The main interaction involves a C-terminal peptide of Pol IV, and is similar to interactions seen between isolated peptides and other processivity factors. However, this first structure of an entire domain of a binding partner with an assembled clamp reveals a substantial secondary interface, which maintains the polymerase in an inactive orientation, and may regulate the switch between replicative and Y-family DNA polymerases in response to a template strand lesion.
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1UNN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UNN OCA].
__TOC__
 
</StructureSection>
==Reference==
Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp., Bunting KA, Roe SM, Pearl LH, EMBO J. 2003 Nov 3;22(21):5883-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14592985 14592985]
[[Category: DNA-directed DNA polymerase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Bunting, K A.]]
[[Category: Bunting KA]]
[[Category: Pearl, L H.]]
[[Category: Pearl LH]]
[[Category: Roe, S M.]]
[[Category: Roe SM]]
[[Category: beta-clamp]]
[[Category: dna replication]]
[[Category: dna-directed dna polymerase]]
[[Category: pol iv]]
[[Category: transferase]]
[[Category: translesion]]
 
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Retrieved from "https://proteopedia.org/1unn"