2fug

==Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus==

==Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus==

== Structural highlights ==

== Structural highlights ==

<table><tr><td colspan='2'>[[2fug]] is a 32 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. The December 2011 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Complex I'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2011_12 10.2210/rcsb_pdb/mom_2011_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FUG FirstGlance]. <br>

<table><tr><td colspan='2'>[[2fug]] is a 32 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. The December 2011 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Complex I'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2011_12 10.2210/rcsb_pdb/mom_2011_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FUG FirstGlance]. <br>

<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=2fug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fug OCA], [http://pdbe.org/2fug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fug RCSB], [http://www.ebi.ac.uk/pdbsum/2fug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fug ProSAT]</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=2fug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fug OCA], [http://pdbe.org/2fug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fug RCSB], [http://www.ebi.ac.uk/pdbsum/2fug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fug ProSAT]</span></td></tr>

</table>

</table>

== Function ==

== Function ==

[[http://www.uniprot.org/uniprot/NQO6_THET8 NQO6_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.[HAMAP-Rule:MF_01356] [[http://www.uniprot.org/uniprot/NQO3_THET8 NQO3_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. [[http://www.uniprot.org/uniprot/NQO9_THET8 NQO9_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The role of the nqo9 subunit appears to provide a 'connecting chain' of two clusters between cluster N5 and the terminal cluster N2, and to stabilize the structure of the complex by interacting with other subunits.[HAMAP-Rule:MF_01351] [[http://www.uniprot.org/uniprot/NQO2_THET8 NQO2_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. [[http://www.uniprot.org/uniprot/NQO1_THET8 NQO1_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The nqo1 subunit contains the NADH-binding site and the primary electron acceptor FMN. [[http://www.uniprot.org/uniprot/NQO4_THET8 NQO4_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The nqo4 subunit may contain the quinone-binding site.[HAMAP-Rule:MF_01358] [[http://www.uniprot.org/uniprot/NQO5_THET8 NQO5_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The nqo5 subunit may be involved in the stabilization of the complex.[HAMAP-Rule:MF_01357]

[[http://www.uniprot.org/uniprot/NQO6_THET8 NQO6_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.[HAMAP-Rule:MF_01356] [[http://www.uniprot.org/uniprot/NQO3_THET8 NQO3_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. [[http://www.uniprot.org/uniprot/NQO9_THET8 NQO9_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The role of the nqo9 subunit appears to provide a 'connecting chain' of two clusters between cluster N5 and the terminal cluster N2, and to stabilize the structure of the complex by interacting with other subunits.[HAMAP-Rule:MF_01351] [[http://www.uniprot.org/uniprot/NQO2_THET8 NQO2_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. [[http://www.uniprot.org/uniprot/NQO1_THET8 NQO1_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The nqo1 subunit contains the NADH-binding site and the primary electron acceptor FMN. [[http://www.uniprot.org/uniprot/NQO4_THET8 NQO4_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The nqo4 subunit may contain the quinone-binding site.[HAMAP-Rule:MF_01358] [[http://www.uniprot.org/uniprot/NQO5_THET8 NQO5_THET8]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The nqo5 subunit may be involved in the stabilization of the complex.[HAMAP-Rule:MF_01357]

Check<jmol>

Check<jmol>

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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>

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<text>to colour the structure by Evolutionary Conservation</text>

<text>to colour the structure by Evolutionary Conservation</text>

</div>

</div>

<div class="pdbe-citations 2fug" style="background-color:#fffaf0;"></div>

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== References ==

== References ==

<references/>

<references/>

</StructureSection>

</StructureSection>

[[Category: Complex I]]

[[Category: Complex I]]

[[Category: RCSB PDB Molecule of the Month]]

[[Category: RCSB PDB Molecule of the Month]]

[[Category: Thet8]]

[[Category: Thet8]]