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3tuz
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tuz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TUZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[3tuz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TUZ FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dhw|3dhw]], [[3dhx|3dhx]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dhw|3dhw]], [[3dhx|3dhx]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0198, JW0194, metI, yaeE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), abc, b0199, JW0195, metN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0198, JW0194, metI, yaeE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), abc, b0199, JW0195, metN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tuz RCSB], [http://www.ebi.ac.uk/pdbsum/3tuz PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tuz RCSB], [http://www.ebi.ac.uk/pdbsum/3tuz PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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. [[http://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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | 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 | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Johnson, E | + | [[Category: Johnson, E]] |
| - | [[Category: Nguyen, P | + | [[Category: Nguyen, P]] |
| - | [[Category: Rees, D C | + | [[Category: Rees, D C]] |
[[Category: Abc-transporter]] | [[Category: Abc-transporter]] | ||
[[Category: Amino-acid transport]] | [[Category: Amino-acid transport]] | ||
Revision as of 00:16, 25 December 2014
Inward facing conformations of the MetNI methionine ABC transporter: CY5 SeMet soak crystal form
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