2hin

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<StructureSection load='2hin' size='340' side='right'caption='[[2hin]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
<StructureSection load='2hin' size='340' side='right'caption='[[2hin]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2hin]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpn15 Bpn15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HIN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2hin]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_N15 Escherichia virus N15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HIN FirstGlance]. <br>
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</td></tr><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>
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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]] 1.05&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cro (gene 39) ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40631 BPN15])</td></tr>
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<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hin OCA], [https://pdbe.org/2hin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hin RCSB], [https://www.ebi.ac.uk/pdbsum/2hin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hin ProSAT]</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=2hin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hin OCA], [https://pdbe.org/2hin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hin RCSB], [https://www.ebi.ac.uk/pdbsum/2hin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hin ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q37964_BPN15 Q37964_BPN15]
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Bacteriophage Cro proteins bind to target DNA as dimers but do not all dimerize with equal strength, and differ in fold in the region of the dimer interface. We report the structure of the Cro protein from Enterobacteria phage N15 at 1.05 A resolution. The subunit fold contains five alpha-helices and is closely similar to the structure of P22 Cro (1.3 A backbone room mean square difference over 52 residues), but quite different from that of lambda Cro, a structurally diverged member of this family with a mixed alpha-helix/beta-sheet fold. N15 Cro crystallizes as a biological dimer with an extensive interface (1303 A(2) change in accessible surface area per dimer) and also dimerizes in solution with a K(d) of 5.1 +/- 1.5 microM. Its dimerization is much stronger than that of its structural homolog P22 Cro, which does not self-associate detectably in solution. Instead, the level of self-association and interfacial area for N15 Cro is similar to that of lambda Cro, even though these two orthologs do not share the same fold and have dimer interfaces that are qualitatively different in structure. The common Cro ancestor is thought to be an all-helical monomer similar to P22 Cro. We propose that two Cro descendants independently developed stronger dimerization by entirely different mechanisms.
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N15 Cro and lambda Cro: orthologous DNA-binding domains with completely different but equally effective homodimer interfaces.,Dubrava MS, Ingram WM, Roberts SA, Weichsel A, Montfort WR, Cordes MH Protein Sci. 2008 May;17(5):803-12. Epub 2008 Mar 27. PMID:18369196<ref>PMID:18369196</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2hin" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bpn15]]
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[[Category: Escherichia virus N15]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cordes, M H]]
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[[Category: Cordes MH]]
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[[Category: Dubrava, M S]]
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[[Category: Dubrava MS]]
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[[Category: Ingram, W M]]
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[[Category: Ingram WM]]
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[[Category: Montfort, W R]]
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[[Category: Montfort WR]]
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[[Category: Roberts, S A]]
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[[Category: Roberts SA]]
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[[Category: Weichsel, A]]
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[[Category: Weichsel A]]
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[[Category: Dimer interface]]
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[[Category: Helix-turn-helix]]
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[[Category: Transcription]]
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[[Category: Transcription factor]]
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Current revision

Structure of N15 Cro at 1.05 A: an ortholog of lambda Cro with a completely different but equally effective dimerization mechanism

PDB ID 2hin

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