View source for 1u7m


==Solution structure of a diiron protein model: Due Ferri(II) turn mutant==
<StructureSection load='1u7m' size='340' side='right'caption='[[1u7m]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1u7m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U7M FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1u7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u7m OCA], [https://pdbe.org/1u7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u7m RCSB], [https://www.ebi.ac.uk/pdbsum/1u7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u7m ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although the analysis and design of turns that connect the strands in antiparallel beta-hairpins has reached an advanced state, much less is known concerning turns between antiparallel helices in helical hairpins. We have conducted an analysis of the structures and sequence preferences of two types of interhelical turns, each of which connects the two helices by a two-residue linker in an alphaL-beta conformation. Based on this analysis, it became apparent that the turn introduced into a designed four-helix bundle protein, DF1, did not occur within an optimal structural context. DF1 is a dimeric model for the diiron class of proteins. A longer loop with a beta-alphaR-beta conformation was inserted between two helices in the protein, and a sequence was chosen to stabilize its conformation. X-ray crystallography and NMR analysis of the protein showed the structure to be in excellent agreement with design.

Analysis and design of turns in alpha-helical hairpins.,Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, DeGrado WF J Mol Biol. 2005 Mar 11;346(5):1441-54. Epub 2005 Jan 13. PMID:15713492<ref>PMID:15713492</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1u7m" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Calhoun JR]]
[[Category: DeGrado WF]]
[[Category: Lahr S]]
[[Category: Lombardi A]]
[[Category: Maglio O]]
[[Category: Nastri F]]
[[Category: Pavone V]]