5o31: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 5o31~~ is ~~ON HOLD until Paper~~ Publication

==Mitochondrial complex I in the deactive state==

== Structural highlights ==

<table><tr><td colspan='2'>[[5o31]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O31 FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.13Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5o31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o31 OCA], [https://pdbe.org/5o31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o31 RCSB], [https://www.ebi.ac.uk/pdbsum/5o31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o31 ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/NDUS5_BOVIN NDUS5_BOVIN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.

== Publication Abstract from PubMed ==

Complex I (NADH:ubiquinone oxidoreductase) is central to energy metabolism in mammalian mitochondria. It couples NADH oxidation by ubiquinone to proton transport across the energy-conserving inner membrane, catalyzing respiration and driving ATP synthesis. In the absence of substrates, active complex I gradually enters a pronounced resting or deactive state. The active-deactive transition occurs during ischemia and is crucial for controlling how respiration recovers upon reperfusion. Here, we set a highly active preparation of Bos taurus complex I into the biochemically defined deactive state, and used single-particle electron cryomicroscopy to determine its structure to 4.1 A resolution. We show that the deactive state arises when critical structural elements that form the ubiquinone-binding site become disordered, and we propose reactivation is induced when substrate binding to the NADH-reduced enzyme templates their reordering. Our structure both rationalizes biochemical data on the deactive state and offers new insights into its physiological and cellular roles.

~~Authors~~:

Structure of the Deactive State of Mammalian Respiratory Complex I.,Blaza JN, Vinothkumar KR, Hirst J Structure. 2018 Feb 6;26(2):312-319.e3. doi: 10.1016/j.str.2017.12.014. Epub 2018, Jan 26. PMID:29395787<ref>PMID:29395787</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</SX>

[[Category: Bos taurus]]

[[Category: Large Structures]]

[[Category: Blaza JN]]

[[Category: Hirst J]]

[[Category: Vinothkumar KR]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5o31 is ON HOLD  until Paper Publication
+==Mitochondrial complex I in the deactive state==
+<SX load='5o31' size='340' side='right' viewer='molstar' caption='[[5o31]], [[Resolution|resolution]] 4.13&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5o31]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O31 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.13&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5o31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o31 OCA], [https://pdbe.org/5o31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o31 RCSB], [https://www.ebi.ac.uk/pdbsum/5o31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o31 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NDUS5_BOVIN NDUS5_BOVIN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Complex I (NADH:ubiquinone oxidoreductase) is central to energy metabolism in mammalian mitochondria. It couples NADH oxidation by ubiquinone to proton transport across the energy-conserving inner membrane, catalyzing respiration and driving ATP synthesis. In the absence of substrates, active complex I gradually enters a pronounced resting or deactive state. The active-deactive transition occurs during ischemia and is crucial for controlling how respiration recovers upon reperfusion. Here, we set a highly active preparation of Bos taurus complex I into the biochemically defined deactive state, and used single-particle electron cryomicroscopy to determine its structure to 4.1 A resolution. We show that the deactive state arises when critical structural elements that form the ubiquinone-binding site become disordered, and we propose reactivation is induced when substrate binding to the NADH-reduced enzyme templates their reordering. Our structure both rationalizes biochemical data on the deactive state and offers new insights into its physiological and cellular roles.
-Authors:
+Structure of the Deactive State of Mammalian Respiratory Complex I.,Blaza JN, Vinothkumar KR, Hirst J Structure. 2018 Feb 6;26(2):312-319.e3. doi: 10.1016/j.str.2017.12.014. Epub 2018, Jan 26. PMID:29395787<ref>PMID:29395787</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5o31" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Bos taurus]]
+[[Category: Large Structures]]
+[[Category: Blaza JN]]
+[[Category: Hirst J]]
+[[Category: Vinothkumar KR]]