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4myc

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==Structure of the mitochondrial ABC transporter, Atm1==
==Structure of the mitochondrial ABC transporter, Atm1==
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<StructureSection load='4myc' size='340' side='right' caption='[[4myc]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
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<StructureSection load='4myc' size='340' side='right'caption='[[4myc]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4myc]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MYC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MYC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4myc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MYC FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4myh|4myh]]</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]] 3.06&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATM1, MDY, YMR301C, YM9952.03C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4myc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myc OCA], [https://pdbe.org/4myc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4myc RCSB], [https://www.ebi.ac.uk/pdbsum/4myc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4myc ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xenobiotic-transporting_ATPase Xenobiotic-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.44 3.6.3.44] </span></td></tr>
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<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=4myc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myc OCA], [http://pdbe.org/4myc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4myc RCSB], [http://www.ebi.ac.uk/pdbsum/4myc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4myc ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ATM1_YEAST ATM1_YEAST]] Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins.<ref>PMID:10406803</ref>
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[https://www.uniprot.org/uniprot/ATM1_YEAST ATM1_YEAST] Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins.<ref>PMID:10406803</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The yeast mitochondrial ABC transporter Atm1, in concert with glutathione, functions in the export of a substrate required for cytosolic-nuclear iron-sulfur protein biogenesis and cellular iron regulation. Defects in the human ortholog ABCB7 cause the sideroblastic anemia XLSA/A. Here, we report the crystal structures of free and glutathione-bound Atm1 in inward-facing, open conformations at 3.06- and 3.38-angstrom resolution, respectively. The glutathione binding site includes a residue mutated in XLSA/A and is located close to the inner membrane surface in a large cavity. The two nucleotide-free adenosine 5'-triphosphate binding domains do not interact yet are kept in close vicinity through tight interaction of the two C-terminal alpha-helices of the Atm1 dimer. The resulting protein stabilization may be a common structural feature of all ABC exporters.
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Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1.,Srinivasan V, Pierik AJ, Lill R Science. 2014 Mar 7;343(6175):1137-40. doi: 10.1126/science.1246729. PMID:24604199<ref>PMID:24604199</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 4myc" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
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[[Category: Large Structures]]
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[[Category: Xenobiotic-transporting ATPase]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Srinivasan, V]]
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[[Category: Srinivasan V]]
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[[Category: Abc transporter]]
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[[Category: Membrane transport]]
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[[Category: Mitochondrial inner membrane]]
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[[Category: Transport protein]]
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Current revision

Structure of the mitochondrial ABC transporter, Atm1

PDB ID 4myc

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