3k8a

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{{STRUCTURE_3k8a| PDB=3k8a | SCENE= }}
 
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===Neisseria gonorrhoeae PriB===
 
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{{ABSTRACT_PUBMED_19906704}}
 
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==About this Structure==
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==Neisseria gonorrhoeae PriB==
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[[3k8a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_fa_1090 Neisseria gonorrhoeae fa 1090]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K8A OCA].
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<StructureSection load='3k8a' size='340' side='right'caption='[[3k8a]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3k8a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_FA_1090 Neisseria gonorrhoeae FA 1090]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K8A FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k8a OCA], [https://pdbe.org/3k8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k8a RCSB], [https://www.ebi.ac.uk/pdbsum/3k8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k8a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRIB_NEIG1 PRIB_NEIG1] Stimulates the DNA unwinding activity of PriA helicase, which does not seem to require single-stranded DNA-binding by PriB. Activates DNA-dependent ATP hydrolysis catalyzed by PriA (PubMed:21861872). Has a weak single-stranded DNA-binding activity (PubMed:21861872, PubMed:19906704). Binds weakly also double-stranded DNA, a partial duplex DNA with a 3' single-stranded DNA overhang, and a forked DNA structure with fully duplex leading and lagging strand arms in vitro (PubMed:21861872).<ref>PMID:19906704</ref> <ref>PMID:21861872</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k8/3k8a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3k8a ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Reactivation of repaired DNA replication forks is essential for complete duplication of bacterial genomes. However, not all bacteria encode homologs of the well-studied Escherichia coli DNA replication restart primosome proteins, suggesting that there might be distinct mechanistic differences among DNA replication restart pathways in diverse bacteria. Since reactivation of repaired DNA replication forks requires coordinated DNA and protein binding by DNA replication restart primosome proteins, we determined the crystal structure of Neisseria gonorrhoeae PriB at 2.7 A resolution and investigated its ability to physically interact with DNA and PriA helicase. Comparison of the crystal structures of PriB from N. gonorrhoeae and E. coli reveals a well-conserved homodimeric structure consisting of two oligosaccharide/oligonucleotide-binding (OB) folds. In spite of their overall structural similarity, there is significant species variation in the type and distribution of surface amino acid residues. This correlates with striking differences in the affinity with which each PriB homolog binds single-stranded DNA and PriA helicase. These results provide evidence that mechanisms of DNA replication restart are not identical across diverse species and that these pathways have likely become specialized to meet the needs of individual organisms.
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==Reference==
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The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways.,Dong J, George NP, Duckett KL, DeBeer MA, Lopper ME Nucleic Acids Res. 2010 Jan;38(2):499-509. Epub 2009 Nov 11. PMID:19906704<ref>PMID:19906704</ref>
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<ref group="xtra">PMID:019906704</ref><references group="xtra"/><references/>
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[[Category: Neisseria gonorrhoeae fa 1090]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: DeBeer, M A.]]
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</div>
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[[Category: Dong, J.]]
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<div class="pdbe-citations 3k8a" style="background-color:#fffaf0;"></div>
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[[Category: Duckett, K L.]]
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== References ==
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[[Category: George, N P.]]
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<references/>
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[[Category: Lopper, M E.]]
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__TOC__
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[[Category: Beta-barrel]]
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</StructureSection>
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[[Category: Dna binding protein]]
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[[Category: Large Structures]]
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[[Category: Ob-fold]]
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[[Category: Neisseria gonorrhoeae FA 1090]]
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[[Category: DeBeer MA]]
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[[Category: Dong J]]
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[[Category: Duckett KL]]
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[[Category: George NP]]
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[[Category: Lopper ME]]

Current revision

Neisseria gonorrhoeae PriB

PDB ID 3k8a

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