|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4wz7' size='340' side='right'caption='[[4wz7]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='4wz7' size='340' side='right'caption='[[4wz7]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wz7]] is a 67 chain structure with sequence from [http://en.wikipedia.org/wiki/Yarrowia_lipolytica Yarrowia lipolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WZ7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wz7]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Yarrowia_lipolytica Yarrowia lipolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZ7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | + | </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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=4wz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wz7 OCA], [https://pdbe.org/4wz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wz7 RCSB], [https://www.ebi.ac.uk/pdbsum/4wz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wz7 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADH:ubiquinone_reductase_(H(+)-translocating) NADH:ubiquinone reductase (H(+)-translocating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.3 1.6.5.3] </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=4wz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wz7 OCA], [http://pdbe.org/4wz7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wz7 RCSB], [http://www.ebi.ac.uk/pdbsum/4wz7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wz7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NU6M_YARLI NU6M_YARLI]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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. [[http://www.uniprot.org/uniprot/NU4LM_YARLI NU4LM_YARLI]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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. | + | [https://www.uniprot.org/uniprot/NU6M_YARLI NU6M_YARLI] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 24: |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Yarrowia lipolytica]] | | [[Category: Yarrowia lipolytica]] |
| - | [[Category: Brandt, U]] | + | [[Category: Brandt U]] |
| - | [[Category: Hunte, C]] | + | [[Category: Hunte C]] |
| - | [[Category: Wirth, C]] | + | [[Category: Wirth C]] |
| - | [[Category: Zickermann, V]] | + | [[Category: Zickermann V]] |
| - | [[Category: Complex i]]
| + | |
| - | [[Category: Mitochondria]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Respiratory chain]]
| + | |
| Structural highlights
Function
NU6M_YARLI Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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
Proton-pumping complex I of the mitochondrial respiratory chain is among the largest and most complicated membrane protein complexes. The enzyme contributes substantially to oxidative energy conversion in eukaryotic cells. Its malfunctions are implicated in many hereditary and degenerative disorders. We report the x-ray structure of mitochondrial complex I at a resolution of 3.6 to 3.9 angstroms, describing in detail the central subunits that execute the bioenergetic function. A continuous axis of basic and acidic residues running centrally through the membrane arm connects the ubiquinone reduction site in the hydrophilic arm to four putative proton-pumping units. The binding position for a substrate analogous inhibitor and blockage of the predicted ubiquinone binding site provide a model for the "deactive" form of the enzyme. The proposed transition into the active form is based on a concerted structural rearrangement at the ubiquinone reduction site, providing support for a two-state stabilization-change mechanism of proton pumping.
Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I.,Zickermann V, Wirth C, Nasiri H, Siegmund K, Schwalbe H, Hunte C, Brandt U Science. 2015 Jan 2;347(6217):44-9. doi: 10.1126/science.1259859. PMID:25554780[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zickermann V, Wirth C, Nasiri H, Siegmund K, Schwalbe H, Hunte C, Brandt U. Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I. Science. 2015 Jan 2;347(6217):44-9. doi: 10.1126/science.1259859. PMID:25554780 doi:http://dx.doi.org/10.1126/science.1259859
|
