View source for 3tuj


==Inward facing conformations of the MetNI methionine ABC transporter: DM crystal form==
<StructureSection load='3tuj' size='340' side='right'caption='[[3tuj]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tuj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUJ 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]] 4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3tuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuj OCA], [https://pdbe.org/3tuj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tuj RCSB], [https://www.ebi.ac.uk/pdbsum/3tuj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/METI_ECOLI METI_ECOLI] Part of the binding-protein-dependent transport system for D-methionine and the toxic methionine analog alpha-methyl-methionine. Probably responsible for the translocation of the substrate across the membrane.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two new crystal structures of the E. coli high affinity methionine uptake ATP Binding Cassette (ABC) transporter MetNI, purified in the detergents cyclohexyl-pentyl-beta-D-maltoside (CY5) and n-decyl-beta-D-maltopyranoside (DM), have been solved in inward facing conformations to resolutions of 2.9 and 4.0 A, respectively. Compared to the previously reported 3.7 A resolution structure of MetNI purified in n-dodecyl-beta-D-maltopyranoside (DDM), the higher resolution of the CY5 data enabled significant improvements to the structural model in several regions, including corrections to the sequence registry, and identification of ADP in the nucleotide binding site. CY5 crystals soaked with selenomethionine established details of the methionine binding site in the C2 regulatory domain of the ABC subunit, including the displacement of the side chain of MetN residue methionine 301 by the exogenous ligand. When compared to the CY5 or DDM structures, the DM structure exhibits a significant repositioning of the dimeric C2 domains, including an unexpected register shift in the intermolecular beta-sheet hydrogen bonding between monomers, and a narrowing of the nucleotide binding space. The immediate proximity of the exogenous methionine binding site to the conformationally variable dimeric interface provides an indication of how methionine binding to the regulatory domains might mediate the phenomenon of transinhibition.

Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition.,Johnson E, Nguyen PT, Yeates TO, Rees DC Protein Sci. 2011 Nov 16. doi: 10.1002/pro.765. PMID:22095702<ref>PMID:22095702</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tuj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Johnson E]]
[[Category: Nguyen P]]
[[Category: Rees DC]]