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3tuz

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<StructureSection load='3tuz' size='340' side='right'caption='[[3tuz]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='3tuz' size='340' side='right'caption='[[3tuz]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tuz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tuz]] is a 8 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=3TUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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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]] 3.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dhw|3dhw]], [[3dhx|3dhx]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0198, JW0194, metI, yaeE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), abc, b0199, JW0195, metN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuz OCA], [https://pdbe.org/3tuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tuz RCSB], [https://www.ebi.ac.uk/pdbsum/3tuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuz ProSAT]</span></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=3tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuz OCA], [https://pdbe.org/3tuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tuz RCSB], [https://www.ebi.ac.uk/pdbsum/3tuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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. [[https://www.uniprot.org/uniprot/METN_ECOLI METN_ECOLI]] Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system (Probable). It has also been shown to be involved in formyl-L-methionine transport.<ref>PMID:12169620</ref> <ref>PMID:12819857</ref>
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3tuz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Johnson, E]]
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[[Category: Johnson E]]
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[[Category: Nguyen, P]]
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[[Category: Nguyen P]]
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[[Category: Rees, D C]]
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[[Category: Rees DC]]
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[[Category: Abc-transporter]]
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[[Category: Amino-acid transport]]
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[[Category: Atp-binding]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-transport protein complex]]
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[[Category: Inner membrane]]
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[[Category: Membrane protein]]
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[[Category: Methionine uptake transporter]]
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[[Category: Type i abc type importer]]
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Current revision

Inward facing conformations of the MetNI methionine ABC transporter: CY5 SeMet soak crystal form

PDB ID 3tuz

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