DP00089: Ubiquinol oxidase subunit 2FASTA viewXML view

General information
DisProt:DP00089
Name:Ubiquinol oxidase subunit 2
Synonym(s):CYOA_ECOLI
Ubiquinol oxidase polypeptide II
Cytochrome o subunit 2
Oxidase BO(3) subunit 2
Cytochrome o ubiquinol oxidase subunit 2
Ubiquinol oxidase chain B
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P0ABJ1
UniGene: 
SwissProt: CYOA_ECOLI
TrEMBL:  
NCBI (GI): 78099990
Source organism:Escherichia coli (strain K12)
Sequence length:315
Percent disordered:19%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MRLRKYNKSL GWLSLFAGTV LLSGCNSALL DPKGQIGLEQ RSLILTAFGL MLIVVIPAIL - 60
MAVGFAWKYR ASNKDAKYSP NWSHSNKVEA VVWTVPILII IFLAVLTWKT THALEPSKPL - 120
AHDEKPITIE VVSMDWKWFF IYPEQGIATV NEIAFPANTP VYFKVTSNSV MNSFFIPRLG - 180
SQIYAMAGMQ TRLHLIANEP GTYDGISASY SGPGFSGMKF KAIATPDRAA FDQWVAKAKQ - 240
SPNTMSDMAA FEKLAAPSEY NQVEYFSNVK PDLFADVINK FMAHGKSMDM TQPEGEHSAH - 300
EGMEGMDMSH AESAH



Functional narrative    

Ubiquinol oxidase polypeptide II is a protein that is one of four subunits. The protein complex catalyzes oxygen reduction into water and uses available free energy to drive a proton gradient across the membrane in the aerobic respiratory chain of E. coli. It belongs to the heme-copper oxidase superfamily of enzymes and the cytochrome c oxidase subunit 2 family. It is a heteroctamer of two A chains, two B chains, two C chains and two D chains. The C-terminal extrinsic domain of subunit II has been proposed to contain a ubiquinone binding site at its interface with subunit I.

Region 3: 1-14 Region 1: 1-26 Region 4: 283-315 Region 2: 284-315

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:1 - 26
Length:26
Region sequence:

MRLRKYNKSLGWLSLFAGTVLLSGCN

Modification type: Engineered
PDB: 1FFT:B, 1FFT:G
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (PEG 1500 (approximate (w/v)) 9 %; sodium chloride 100 mM; magnesium chloride 100 mM; ethanol ((v/v)) 5 %)

References:
  1. Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol. 2000; 7(10): 910-7. PubMed: 11017202

Comments:
This region is located in the periplasmic space.


Abramson et al. could not assign a sequence for residues 1-36 or 113-124. However the PDB file locates electron density for residues 27-283.




Region 2
Type:Disordered
Name: 
Location:284 - 315
Length:32
Region sequence:

HGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH

Modification type: Engineered
PDB: 1FFT:B, 1FFT:G
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (ethanol ((v/v)) 5 %; magnesium chloride 100 mM; PEG 1500 (approximate (w/v)) 9 %; sodium chloride 100 mM)

References:
  1. Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol. 2000; 7(10): 910-7. PubMed: 11017202

Comments:
This region is located in the periplasmic space.




Region 3
Type:Disordered
Name: 
Location:1 - 14
Length:14
Region sequence:

MRLRKYNKSLGWLS

Modification type: Fragment
PDB: 1FFT:B, 1FFT:G
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (277 K; ammonium sulfate (precipitant) 35 %; citrate/bis-Tris-propane ((pH 9.0-9.5)) 100 mM; dimethylsulphoxide ((to obtain sharp edges) v/v) 2 %; DTT (buffer) 1 mM; EDTA (buffer) 1 mM; NaN3 (buffer) 1 mM)

References:
  1. van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmstrom BG, et al. "Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex." Embo J. 1992; 11(9): 3209-17. PubMed: 1324168

  2. van der Oost J, Musacchio A, Pauptit RA, Ceska TA, Wierenga RK, Saraste M. "Crystallization and preliminary X-ray analysis of the periplasmic fragment of CyoA-a subunit of the Escherichia coli cytochrome o complex." J Mol Biol. 1993; 229(3): 794-6. PubMed: 8433374

  3. Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M. "Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center." Proc Natl Acad Sci U S A. 1995; 92(26): 11955-9. PubMed: 8618822

Comments:
This region is located in the periplasmic space.




Region 4
Type:Disordered
Name: 
Location:283 - 315
Length:33
Region sequence:

AHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH

Modification type: Fragment
PDB: 1FFT:B, 1FFT:G
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (277 K; ammonium sulfphate (precipitant) 35 %; citrate/bis-Tris-propane ((pH 9.0-9.5)) 100 mM; dimethylsuphoxide ((to obtain sharp edges) v/v) 2 %; DTT (buffer) 1 mM; EDTA (buffer) 1 mM; NaN3 (buffer) 1 mM)

References:
  1. van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmstrom BG, et al. "Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex." Embo J. 1992; 11(9): 3209-17. PubMed: 1324168

  2. van der Oost J, Musacchio A, Pauptit RA, Ceska TA, Wierenga RK, Saraste M. "Crystallization and preliminary X-ray analysis of the periplasmic fragment of CyoA-a subunit of the Escherichia coli cytochrome o complex." J Mol Biol. 1993; 229(3): 794-6. PubMed: 8433374

  3. Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M. "Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center." Proc Natl Acad Sci U S A. 1995; 92(26): 11955-9. PubMed: 8618822

Comments:
This region is located in the periplasmic space.




References

  1. Chepuri V, Lemieux L, Au DC, Gennis RB. "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem. 1990; 265(19): 11185-92. PubMed: 2162835



Comments


A periplasmic fragment of subunit II is located under the PDB identification of 1CYW. It is residues 125-283 of subunit II as described by Abramson et. al.


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