9sej: Difference between revisions

Latest revision as of 06:34, 22 April 2026

E.coli cytochrome bd-I dimer bound to Aurachin D

Structural highlights

9sej is a 8 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.47Å
Ligands:	0NI, HEM, LPP, OXY, PGT, POV, UQ8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYDA_ECOLI A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.^[1] ^[2] ^[3] ^[4] ^[5]

References

↑ Bekker M, de Vries S, Ter Beek A, Hellingwerf KJ, de Mattos MJ. Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase. J Bacteriol. 2009 Sep;191(17):5510-7. doi: 10.1128/JB.00562-09. Epub 2009 Jun 19. PMID:19542282 doi:https://dx.doi.org/10.1128/JB.00562-09
↑ Borisov VB, Murali R, Verkhovskaya ML, Bloch DA, Han H, Gennis RB, Verkhovsky MI. Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc Natl Acad Sci U S A. 2011 Oct 18;108(42):17320-4. doi:, 10.1073/pnas.1108217108. Epub 2011 Oct 10. PMID:21987791 doi:https://dx.doi.org/10.1073/pnas.1108217108
↑ Fang H, Lin RJ, Gennis RB. Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis. J Biol Chem. 1989 May 15;264(14):8026-32. PMID:2656671
↑ Miller MJ, Gennis RB. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J Biol Chem. 1983 Aug 10;258(15):9159-65. PMID:6307994
↑ Kaysser TM, Ghaim JB, Georgiou C, Gennis RB. Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli. Biochemistry. 1995 Oct 17;34(41):13491-501. doi: 10.1021/bi00041a029. PMID:7577938 doi:https://dx.doi.org/10.1021/bi00041a029

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Bekker M, de Vries S, Ter Beek A, Hellingwerf KJ, de Mattos MJ. Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase. J Bacteriol. 2009 Sep;191(17):5510-7. doi: 10.1128/JB.00562-09. Epub 2009 Jun 19. PMID:19542282 doi:https://dx.doi.org/10.1128/JB.00562-09

[2] Borisov VB, Murali R, Verkhovskaya ML, Bloch DA, Han H, Gennis RB, Verkhovsky MI. Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc Natl Acad Sci U S A. 2011 Oct 18;108(42):17320-4. doi:, 10.1073/pnas.1108217108. Epub 2011 Oct 10. PMID:21987791 doi:https://dx.doi.org/10.1073/pnas.1108217108

[3] Fang H, Lin RJ, Gennis RB. Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis. J Biol Chem. 1989 May 15;264(14):8026-32. PMID:2656671

[4] Miller MJ, Gennis RB. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J Biol Chem. 1983 Aug 10;258(15):9159-65. PMID:6307994

[5] Kaysser TM, Ghaim JB, Georgiou C, Gennis RB. Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli. Biochemistry. 1995 Oct 17;34(41):13491-501. doi: 10.1021/bi00041a029. PMID:7577938 doi:https://dx.doi.org/10.1021/bi00041a029

[1]

[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9sej is ON HOLD  until Paper Publication
+==E.coli cytochrome bd-I dimer bound to Aurachin D==
+<StructureSection load='9sej' size='340' side='right'caption='[[9sej]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
-Authors: van der Velden, T.T., Kaystha, K., Bruenle, S., Jeuken, L.J.C.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9sej]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9SEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9SEJ FirstGlance]. <br>
-Description: E.coli cytochrome bd-I dimer bound to Aurachin D
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.47&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0NI:2-methyl-3-[(6~{E})-3,7,11-trimethyldodeca-2,6,10-trienyl]-1~{H}-quinolin-4-one'>0NI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LPP:2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+HEXADECANOATE'>LPP</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PGT:(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PGT</scene>, <scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</scene>, <scene name='pdbligand=UQ8:UBIQUINONE-8'>UQ8</scene></td></tr>
-[[Category: Van Der Velden, T.T]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9sej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9sej OCA], [https://pdbe.org/9sej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9sej RCSB], [https://www.ebi.ac.uk/pdbsum/9sej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9sej ProSAT]</span></td></tr>
-[[Category: Kaystha, K]]
+</table>
-[[Category: Bruenle, S]]
+== Function ==
-[[Category: Jeuken, L.J.C]]
+[https://www.uniprot.org/uniprot/CYDA_ECOLI CYDA_ECOLI] A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.<ref>PMID:19542282</ref> <ref>PMID:21987791</ref> <ref>PMID:2656671</ref> <ref>PMID:6307994</ref> <ref>PMID:7577938</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Bruenle S]]
+[[Category: Jeuken LJC]]
+[[Category: Kaystha K]]
+[[Category: Van der Velden TT]]

9sej: Difference between revisions

Latest revision as of 06:34, 22 April 2026

E.coli cytochrome bd-I dimer bound to Aurachin D

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools