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==The crystal structure of the bacteriophage T4 MotA C-terminal domain in complex with dsDNA reveals a novel protein-DNA recognition motif==
<StructureSection load='5jlt' size='340' side='right'caption='[[5jlt]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jlt]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JLT 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]] 2.955&#8491;</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=5jlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jlt OCA], [https://pdbe.org/5jlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jlt RCSB], [https://www.ebi.ac.uk/pdbsum/5jlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jlt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MOTA_BPT4 MOTA_BPT4] Required for the transcriptional activation of middle promoters. Middle promoters are characterized by the presence of the conserved sequence [AT]3TGCTTNA (MotA box). MotA binds directly to MotA boxes.
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== Publication Abstract from PubMed ==
During infection, bacteriophage T4 produces the MotA transcription factor that redirects the host RNA polymerase to the expression of T4 middle genes. The C-terminal 'double-wing' domain of MotA binds specifically to the MotA box motif of middle T4 promoters. We report the crystal structure of this complex, which reveals a new mode of protein-DNA interaction. The domain binds DNA mostly via interactions with the DNA backbone, but the binding is enhanced in the specific cognate structure by additional interactions with the MotA box motif in both the major and minor grooves. The linker connecting the two MotA domains plays a key role in stabilizing the complex via minor groove interactions. The structure is consistent with our previous model derived from chemical cleavage experiments using the entire transcription complex. alpha- and beta-d-glucosyl-5-hydroxymethyl-deoxycytosine replace cytosine in T4 DNA, and docking simulations indicate that a cavity in the cognate structure can accommodate the modified cytosine. Binding studies confirm that the modification significantly enhances the binding affinity of MotA for the DNA. Consequently, our work reveals how a DNA modification can extend the uniqueness of small DNA motifs to facilitate the specificity of protein-DNA interactions.

The phage T4 MotA transcription factor contains a novel DNA binding motif that specifically recognizes modified DNA.,Cuypers MG, Robertson RM, Knipling L, Waddell MB, Moon K, Hinton DM, White SW Nucleic Acids Res. 2018 Jun 1;46(10):5308-5318. doi: 10.1093/nar/gky292. PMID:29718457<ref>PMID:29718457</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Cuypers MG]]
[[Category: Hinton DM]]
[[Category: Knipling L]]
[[Category: Robertson RM]]
[[Category: White SW]]