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| | <StructureSection load='6odd' size='340' side='right'caption='[[6odd]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6odd' size='340' side='right'caption='[[6odd]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6odd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ODD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ODD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6odd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ODD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ODD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8Q1:S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]+dodecanethioate'>8Q1</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NDUFAB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), LYRM4, C6orf149, ISD11, CGI-203 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8Q1:S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]+dodecanethioate'>8Q1</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=6odd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6odd OCA], [http://pdbe.org/6odd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6odd RCSB], [http://www.ebi.ac.uk/pdbsum/6odd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6odd 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=6odd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6odd OCA], [https://pdbe.org/6odd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6odd RCSB], [https://www.ebi.ac.uk/pdbsum/6odd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6odd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | == Disease == | |
| - | [[http://www.uniprot.org/uniprot/LYRM4_HUMAN LYRM4_HUMAN]] Severe neonatal lactic acidosis due to NFS1-ISD11 complex deficiency. The disease is caused by mutations affecting the gene represented in this entry. | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACPM_HUMAN ACPM_HUMAN]] Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). [[http://www.uniprot.org/uniprot/LYRM4_HUMAN LYRM4_HUMAN]] Required for nuclear and mitochondrial iron-sulfur protein biosynthesis.<ref>PMID:17331979</ref> <ref>PMID:19454487</ref> | + | [https://www.uniprot.org/uniprot/ACPM_HUMAN ACPM_HUMAN] Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6odd" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6odd" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Herrera, M G]] | + | [[Category: Herrera MG]] |
| - | [[Category: Klinke, S]] | + | [[Category: Klinke S]] |
| - | [[Category: Noguera, M E]] | + | [[Category: Noguera ME]] |
| - | [[Category: Santos, J]] | + | [[Category: Santos J]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Cysteine desulfurase activity regulator]]
| + | |
| - | [[Category: Iron sulfur cluster]]
| + | |
| Structural highlights
Function
ACPM_HUMAN Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity).
Publication Abstract from PubMed
In recent years, the mammalian mitochondrial protein complex for iron-sulfur cluster assembly has been the focus of important studies. This is partly because of its high degree of relevance in cell metabolism and because mutations of the involved proteins are the cause of several human diseases. Cysteine desulfurase NFS1 is the key enzyme of the complex. At present, it is well-known that the active form of NFS1 is stabilized by the small protein ISD11. In this work, the structure of the human mitochondrial ACP-ISD11 heterodimer was determined at 2.0 A resolution. ACP-ISD11 forms a cooperative unit stabilized by several ionic interactions, hydrogen bonds, and apolar interactions. The 4'-phosphopantetheine-acyl chain, which is covalently bound to ACP, interacts with several residues of ISD11, modulating together with ACP the foldability of ISD11. Recombinant human ACP-ISD11 was able to interact with the NFS1 desulfurase, thus yielding an active enzyme, and the NFS1/ACP-ISD11 core complex was activated by frataxin and ISCU proteins. Internal motions of ACP-ISD11 were studied by molecular dynamics simulations, showing the persistence of the interactions between both protein chains. The conformation of the dimer is similar to that found in the context of the (NFS1/ACP-ISD11)2 supercomplex core, which contains the Escherichia coli ACP instead of the human variant. This fact suggests a sequential mechanism for supercomplex consolidation, in which the ACP-ISD11 complex may fold independently and, after that, the NFS1 dimer would be stabilized.
Structure of the Human ACP-ISD11 Heterodimer.,Herrera MG, Noguera ME, Sewell KE, Agudelo Suarez WA, Capece L, Klinke S, Santos J Biochemistry. 2019 Nov 19;58(46):4596-4609. doi: 10.1021/acs.biochem.9b00539., Epub 2019 Nov 8. PMID:31664822[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Herrera MG, Noguera ME, Sewell KE, Agudelo Suarez WA, Capece L, Klinke S, Santos J. Structure of the Human ACP-ISD11 Heterodimer. Biochemistry. 2019 Nov 19;58(46):4596-4609. doi: 10.1021/acs.biochem.9b00539., Epub 2019 Nov 8. PMID:31664822 doi:http://dx.doi.org/10.1021/acs.biochem.9b00539
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