4h2d: Difference between revisions
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==Crystal structure of NDOR1== | |||
=== | <StructureSection load='4h2d' size='340' side='right' caption='[[4h2d]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4h2d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H2D FirstGlance]. <br> | |||
==Function== | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ja1|1ja1]], [[1j9z|1j9z]], [[1ykg|1ykg]], [[1es9|1es9]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NDOR1, NR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4h2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h2d RCSB], [http://www.ebi.ac.uk/pdbsum/4h2d PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/NDOR1_HUMAN NDOR1_HUMAN]] Oxidoreductase that catalyzes the NADP-dependent reduction of cytochrome c and one-electron acceptors, such as doxorubicin, potassium ferricyanide and menadione (in vitro).<ref>PMID:10625700</ref> | [[http://www.uniprot.org/uniprot/NDOR1_HUMAN NDOR1_HUMAN]] Oxidoreductase that catalyzes the NADP-dependent reduction of cytochrome c and one-electron acceptors, such as doxorubicin, potassium ferricyanide and menadione (in vitro).<ref>PMID:10625700</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Biogenesis of iron-sulfur cluster proteins is a highly regulated process that requires complex protein machineries. In the cytosolic iron-sulfur protein assembly machinery, two human key proteins-NADPH-dependent diflavin oxidoreductase 1 (Ndor1) and anamorsin-form a stable complex in vivo that was proposed to provide electrons for assembling cytosolic iron-sulfur cluster proteins. The Ndor1-anamorsin interaction was also suggested to be implicated in the regulation of cell survival/death mechanisms. In the present work we unravel the molecular basis of recognition between Ndor1 and anamorsin and of the electron transfer process. This is based on the structural characterization of the two partner proteins, the investigation of the electron transfer process, and the identification of those protein regions involved in complex formation and those involved in electron transfer. We found that an unstructured region of anamorsin is essential for the formation of a specific and stable protein complex with Ndor1, whereas the C-terminal region of anamorsin, containing the [2Fe-2S] redox center, transiently interacts through complementary charged residues with the FMN-binding site region of Ndor1 to perform electron transfer. Our results propose a molecular model of the electron transfer process that is crucial for understanding the functional role of this interaction in human cells. | |||
Molecular view of an electron transfer process essential for iron-sulfur protein biogenesis.,Banci L, Bertini I, Calderone V, Ciofi-Baffoni S, Giachetti A, Jaiswal D, Mikolajczyk M, Piccioli M, Winkelmann J Proc Natl Acad Sci U S A. 2013 Apr 17. PMID:23596212<ref>PMID:23596212</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Banci, L | [[Category: Banci, L]] | ||
[[Category: Bertini, I | [[Category: Bertini, I]] | ||
[[Category: Calderone, V | [[Category: Calderone, V]] | ||
[[Category: Ciofi-Baffoni, S | [[Category: Ciofi-Baffoni, S]] | ||
[[Category: Jaiswal, D | [[Category: Jaiswal, D]] | ||
[[Category: Mikolajczyk, M | [[Category: Mikolajczyk, M]] | ||
[[Category: Winkelmann, J]] | [[Category: Winkelmann, J]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 19:06, 25 December 2014
Crystal structure of NDOR1Crystal structure of NDOR1
Structural highlights
Function[NDOR1_HUMAN] Oxidoreductase that catalyzes the NADP-dependent reduction of cytochrome c and one-electron acceptors, such as doxorubicin, potassium ferricyanide and menadione (in vitro).[1] Publication Abstract from PubMedBiogenesis of iron-sulfur cluster proteins is a highly regulated process that requires complex protein machineries. In the cytosolic iron-sulfur protein assembly machinery, two human key proteins-NADPH-dependent diflavin oxidoreductase 1 (Ndor1) and anamorsin-form a stable complex in vivo that was proposed to provide electrons for assembling cytosolic iron-sulfur cluster proteins. The Ndor1-anamorsin interaction was also suggested to be implicated in the regulation of cell survival/death mechanisms. In the present work we unravel the molecular basis of recognition between Ndor1 and anamorsin and of the electron transfer process. This is based on the structural characterization of the two partner proteins, the investigation of the electron transfer process, and the identification of those protein regions involved in complex formation and those involved in electron transfer. We found that an unstructured region of anamorsin is essential for the formation of a specific and stable protein complex with Ndor1, whereas the C-terminal region of anamorsin, containing the [2Fe-2S] redox center, transiently interacts through complementary charged residues with the FMN-binding site region of Ndor1 to perform electron transfer. Our results propose a molecular model of the electron transfer process that is crucial for understanding the functional role of this interaction in human cells. Molecular view of an electron transfer process essential for iron-sulfur protein biogenesis.,Banci L, Bertini I, Calderone V, Ciofi-Baffoni S, Giachetti A, Jaiswal D, Mikolajczyk M, Piccioli M, Winkelmann J Proc Natl Acad Sci U S A. 2013 Apr 17. PMID:23596212[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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