2hdd

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(New page: 200px<br /><applet load="2hdd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hdd, resolution 1.900&Aring;" /> '''ENGRAILED HOMEODOMA...)
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[[Image:2hdd.gif|left|200px]]<br /><applet load="2hdd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2hdd, resolution 1.900&Aring;" />
 
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'''ENGRAILED HOMEODOMAIN Q50K VARIANT DNA COMPLEX'''<br />
 
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==Overview==
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==ENGRAILED HOMEODOMAIN Q50K VARIANT DNA COMPLEX==
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BACKGROUND: The homeodomain is one of the key DNA-binding motifs used in, eukaryotic gene regulation, and homeodomain proteins play critical roles, in development. The residue at position 50 of many homeodomains appears to, determine the differential DNA-binding specificity, helping to distinguish, among binding sites of the form TAATNN. However, the precise role(s) of, residue 50 in the differential recognition of alternative sites has not, been clear. None of the previously determined structures of, homeodomain-DNA complexes has shown evidence for a stable hydrogen bond, between residue 50 and a base, and there has been much discussion, based, in part on NMR studies, about the potential importance of water-mediated, contacts. This study was initiated to help clarify some of these issues., RESULTS: The crystal structure of a complex containing the engrailed, Gln50--&gt;Lys variant (QK50) with its optimal binding site TAATCC (versus, TAATTA for the wild-type protein) has been determined at 1.9 A resolution., The overall structure of the QK50 variant is very similar to that of the, wild-type complex, but the sidechain of Lys50 projects directly into the, major groove and makes several hydrogen bonds to the O6 and N7 atoms of, the guanines at base pairs 5 and 6. Lys50 also makes an additional, water-mediated contact with the guanine at base pair 5 and has an, alternative conformation that allows a hydrogen bond with the O4 of the, thymine at base pair 4. CONCLUSIONS: The structural context provided by, the folding and docking of the engrailed homeodomain allows Lys50 to make, remarkably favorable contacts with the guanines at base pairs 5 and 6 of, the binding site. Although many different residues occur at position 50 in, different homeodomains, and although numerous position 50 variants have, been constructed, the most striking examples of altered specificity, usually involve introducing or removing a lysine sidechain from position, 50. This high-resolution structure also confirms the critical role of, Asn51 in homeodomain-DNA recognition and further clarifies the roles of, water molecules near residues 50 and 51.
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<StructureSection load='2hdd' size='340' side='right'caption='[[2hdd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2hdd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HDD FirstGlance]. <br>
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2HDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HDD OCA].
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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]] 1.9&#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=2hdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hdd OCA], [https://pdbe.org/2hdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hdd RCSB], [https://www.ebi.ac.uk/pdbsum/2hdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hdd ProSAT]</span></td></tr>
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==Reference==
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</table>
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Engrailed (Gln50--&gt;Lys) homeodomain-DNA complex at 1.9 A resolution: structural basis for enhanced affinity and altered specificity., Tucker-Kellogg L, Rould MA, Chambers KA, Ades SE, Sauer RT, Pabo CO, Structure. 1997 Aug 15;5(8):1047-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9309220 9309220]
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== Function ==
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[https://www.uniprot.org/uniprot/HMEN_DROME HMEN_DROME] This protein specifies the body segmentation pattern. It is required for the development of the central nervous system. Transcriptional regulator that represses activated promoters. Wg signaling operates by inactivating the SGG repression of EN autoactivation.
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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/hd/2hdd_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=2hdd ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ades, S.E.]]
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[[Category: Ades SE]]
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[[Category: Chambers, K.A.]]
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[[Category: Chambers KA]]
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[[Category: Pabo, C.O.]]
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[[Category: Pabo CO]]
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[[Category: Rould, M.A.]]
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[[Category: Rould MA]]
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[[Category: Sauer, R.T.]]
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[[Category: Sauer RT]]
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[[Category: Tucker-Kellogg, L.]]
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[[Category: Tucker-Kellogg L]]
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[[Category: complex (dna binding protein/dna)]]
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[[Category: dna binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:41:16 2007''
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Current revision

ENGRAILED HOMEODOMAIN Q50K VARIANT DNA COMPLEX

PDB ID 2hdd

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