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1ka8

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[[Image:1ka8.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of the Phage P4 Origin-Binding Domain==
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|PDB= 1ka8 |SIZE=350|CAPTION= <scene name='initialview01'>1ka8</scene>, resolution 2.95&Aring;
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<StructureSection load='1ka8' size='340' side='right'caption='[[1ka8]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1ka8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_P4 Enterobacteria phage P4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KA8 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.95&#8491;</td></tr>
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|GENE=
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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=1ka8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ka8 OCA], [https://pdbe.org/1ka8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ka8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ka8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ka8 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''Crystal Structure of the Phage P4 Origin-Binding Domain'''
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[https://www.uniprot.org/uniprot/PRIM_BPP4 PRIM_BPP4] This protein acts as a DNA primase generating di- to pentaribonucleotides; the predominant product being the dimer pppApG. It complexes specifically to the P4 origin of replication (ori) and its cis replication region (crr). It also acts as a DNA helicase.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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The origin-binding domain of the gpalpha protein of phage P4 (P4-OBD) mediates origin recognition and regulation of gpalpha activity by the protein Cnr. We have determined the crystal structure of P4-OBD at 2.95 A resolution. The structure of P4-OBD is that of a dimer with pseudo twofold symmetry. Each subunit has a winged helix topology with a unique structure among initiator proteins. The only structural homologue of the P4-OBD subunit is the DNA-binding domain of the eukaryotic transcriptional activator Rfx1. Based on this structural alignment, a model for origin recognition by the P4-OBD dimer is suggested. P4-OBD mutations that interfere with Cnr binding locate to the dimer interface, indicating that Cnr acts by disrupting the gpalpha dimer. P4-OBD dimerization is mediated by helices alpha1 and alpha3 in both subunits, a mode of winged helix protein dimerization that is reminiscent of that of the eukaryotic transcription factors E2F and DP. This, in turn, suggests that Cnr is also a winged helix protein, a possibility that is supported by previously unreported sequence homologies between Cnr and Rfx1 and homology modelling. Hence, in a mechanism that appears to be conserved from phage to man, the DNA-binding activity of winged helix proteins can be regulated by other winged helix proteins via the versatile use of the winged helix motif as a homo- or heterodimerization scaffold.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ka/1ka8_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1KA8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KA8 OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=1ka8 ConSurf].
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Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins., Yeo HJ, Ziegelin G, Korolev S, Calendar R, Lanka E, Waksman G, Mol Microbiol. 2002 Feb;43(4):855-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11929537 11929537]
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<div style="clear:both"></div>
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[[Category: Enterobacteria phage p21]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Calendar, R.]]
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[[Category: Enterobacteria phage P4]]
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[[Category: Korolev, S.]]
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[[Category: Large Structures]]
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[[Category: Lanka, E.]]
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[[Category: Calendar R]]
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[[Category: Waksman, G.]]
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[[Category: Korolev S]]
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[[Category: Yeo, H J.]]
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[[Category: Lanka E]]
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[[Category: Ziegelin, G.]]
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[[Category: Waksman G]]
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[[Category: winged helix]]
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[[Category: Yeo HJ]]
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[[Category: Ziegelin G]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:14:41 2008''
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Current revision

Crystal Structure of the Phage P4 Origin-Binding Domain

PDB ID 1ka8

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