View source for 2m67


==Full-length mercury transporter protein MerF in lipid bilayer membranes==
<StructureSection load='2m67' size='340' side='right'caption='[[2m67]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Morganella_morganii Morganella morganii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M67 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=2m67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m67 OCA], [https://pdbe.org/2m67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m67 RCSB], [https://www.ebi.ac.uk/pdbsum/2m67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m67 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q56446_MORMO Q56446_MORMO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of the 81-residue mercury transporter MerF determined in liquid crystalline phospholipid bilayers under physiological conditions by Rotationally Aligned (RA) solid-state NMR has two long helices, which extend well beyond the bilayer, with a well-defined interhelical loop. Truncation of the N-terminal 12 residues, which are mobile and unstructured when the protein is solubilized in micelles, results in a large structural rearrangement of the protein in bilayers. In the full-length protein, the N-terminal helix is aligned nearly parallel to the membrane normal and forms an extension of the first transmembrane helix. By contrast, this helix adopts a perpendicular orientation in the truncated protein. The close spatial proximity of the two Cys-containing metal binding sites in the three-dimensional structure of full-length MerF provides insights into possible transport mechanisms. These results demonstrate that major changes in protein structure can result from differences in amino acid sequence (e.g., full-length vs truncated proteins) as well as the use of a non-native membrane mimetic environment (e.g., micelles) vs liquid crystalline phospholipid bilayers. They provide further evidence of the importance of studying unmodified membrane proteins in near-native bilayer environments in order to obtain accurate structures that can be related to their functions.

The Structure of the Mercury Transporter MerF in Phospholipid Bilayers: A Large Conformational Rearrangement Results from N-Terminal Truncation.,Lu GJ, Tian Y, Vora N, Marassi FM, Opella SJ J Am Chem Soc. 2013 Jun 26;135(25):9299-302. doi: 10.1021/ja4042115. Epub 2013, Jun 17. PMID:23763519<ref>PMID:23763519</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m67" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Morganella morganii]]
[[Category: Lu GJ]]
[[Category: Marassi FM]]
[[Category: Opella SJ]]
[[Category: Tian Y]]
[[Category: Vora N]]