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- PDB-2n18: Dominant form of the low-affinity complex of yeast cytochrome c a... -

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Basic information

Entry
Database: PDB / ID: 2n18
TitleDominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase
Components
  • (Cytochrome c iso-1) x 2
  • Cytochrome c peroxidase, mitochondrial
KeywordsOXIDOREDUCTASE/ELECTRON TRANSPORT / cytochrome c / cytochrome c peroxidase / low affinity complex / OXIDOREDUCTASE-ELECTRON TRANSPORT complex
Function / homology
Function and homology information


Release of apoptotic factors from the mitochondria / Pyroptosis / Respiratory electron transport / Detoxification of Reactive Oxygen Species / cytochrome-c peroxidase / cytochrome-c peroxidase activity / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / : / response to reactive oxygen species ...Release of apoptotic factors from the mitochondria / Pyroptosis / Respiratory electron transport / Detoxification of Reactive Oxygen Species / cytochrome-c peroxidase / cytochrome-c peroxidase activity / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / : / response to reactive oxygen species / hydrogen peroxide catabolic process / mitochondrial intermembrane space / peroxidase activity / cellular response to oxidative stress / electron transfer activity / mitochondrial matrix / heme binding / mitochondrion / metal ion binding
Similarity search - Function
Cytochrome c, class IA/ IB / Class I peroxidase / Heme-binding peroxidase Ccp1-like / Cytochrome c / Peroxidase; domain 2 / Peroxidase, domain 2 / Peroxidase; domain 1 - #10 / Cytochrome c-like domain / Peroxidase; domain 1 / Cytochrome Bc1 Complex; Chain D, domain 2 ...Cytochrome c, class IA/ IB / Class I peroxidase / Heme-binding peroxidase Ccp1-like / Cytochrome c / Peroxidase; domain 2 / Peroxidase, domain 2 / Peroxidase; domain 1 - #10 / Cytochrome c-like domain / Peroxidase; domain 1 / Cytochrome Bc1 Complex; Chain D, domain 2 / Peroxidases heam-ligand binding site / Peroxidase, active site / Peroxidases active site signature. / Plant heme peroxidase family profile. / Haem peroxidase / Peroxidase / Peroxidases proximal heme-ligand signature. / Haem peroxidase superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
HEME C / PROTOPORPHYRIN IX CONTAINING FE / Cytochrome c isoform 1 / Cytochrome c peroxidase, mitochondrial
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodSOLUTION NMR / simulated annealing
AuthorsVolkov, A. / Van de Water, K.
CitationJournal: Nat Commun / Year: 2015
Title: The low-affinity complex of cytochrome c and its peroxidase.
Authors: Van de Water, K. / Sterckx, Y.G. / Volkov, A.N.
History
DepositionMar 24, 2015Deposition site: BMRB / Processing site: RCSB
Revision 1.0May 13, 2015Provider: repository / Type: Initial release
Revision 1.1May 20, 2015Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cytochrome c peroxidase, mitochondrial
B: Cytochrome c iso-1
C: Cytochrome c iso-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,5446
Polymers57,6913
Non-polymers1,8533
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4660 Å2
ΔGint-80 kcal/mol
Surface area23340 Å2
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Cytochrome c peroxidase, mitochondrial / CCP


Mass: 33543.188 Da / Num. of mol.: 1 / Fragment: UNP residues 68-361 / Mutation: C128A, V197C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: CCP1, CCP, CPO, YKR066C / Plasmid: pET24 / Production host: Escherichia coli (E. coli) / References: UniProt: P00431, cytochrome-c peroxidase
#2: Protein Cytochrome c iso-1


Mass: 12073.835 Da / Num. of mol.: 1 / Fragment: UNP residues 3-109 / Mutation: A81C, C102T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: CYC1, YJR048W, J1653 / Plasmid: pUCcc / Production host: Escherichia coli (E. coli) / References: UniProt: P00044
#3: Protein Cytochrome c iso-1


Mass: 12073.835 Da / Num. of mol.: 1 / Fragment: UNP residues 2-109
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: CYC1, YJR048W, J1653 / Plasmid: pUCcc / Production host: Escherichia coli (E. coli) / References: UniProt: P00044
#4: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#5: Chemical ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H34FeN4O4

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D 1H-15N HSQC

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Sample preparation

DetailsContents: 0.4 mM [U-2H; U-15N] CcP, 0.4 mM Cc, 0.4 mM Cc1, 20 mM sodium phosphate, 93% H2O/7% D2O
Solvent system: 93% H2O/7% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.4 mMCcP-1[U-2H; U-15N]1
0.4 mMCc-21
0.4 mMCc1-31
20 mMsodium phosphate-41
Sample conditionsIonic strength: 15 / pH: 6.0 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Varian Uniform NMR System / Manufacturer: Varian / Model: Uniform NMR System / Field strength: 800 MHz

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Processing

NMR software
NameDeveloperClassification
VNMRJVariancollection
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
CcpNMRCCPNpeak picking
CcpNMRCCPNchemical shift assignment
CcpNMRCCPNdata analysis
X-PLOR_NIHSchwieters, Kuszewski, Tjandra and Clorestructure solution
X-PLOR_NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: AUTHORS STATE THAT CCP (CHAIN A) HAS TWO BINDING SITES FOR CC (CHAINS B AND C). ONE OF THE SITES IS BLOCKED BY PREPARING A COVALENT CCP-CC CROSSLINK (CHAINS A-B), WHILE STUDYING THE BINDING ...Details: AUTHORS STATE THAT CCP (CHAIN A) HAS TWO BINDING SITES FOR CC (CHAINS B AND C). ONE OF THE SITES IS BLOCKED BY PREPARING A COVALENT CCP-CC CROSSLINK (CHAINS A-B), WHILE STUDYING THE BINDING OF THE SECOND CC MOLECULE (CHAIN C) TO ANOTHER SITE. THE CROSS-LINKING WAS DONE VIA AN ENGINEERED DISULFIDE BETWEEN CCP V197C AND CC A81C GROUPS (I.E. CHAIN A V197C - CHAIN B A81C). IN ADDITION, THE NATIVE CYS RESIDUES OF BOTH CCP AND CC WERE MUTATED OUT (I.E. CHAIN A C128A AND CHAIN B C102T MUTATIONS). THE CROSSLINK STRUCTURE (CHAINS A-B), TAKEN FROM THE PDB ENTRY 1S6V, WAS KEPT FIXED IN THE NMR RESTRAINT-DRIVEN RIGID-BODY DOCKING OF THE SECOND CC MOLECULE (CHAIN C). RIGID-BODY REFINEMENT PROTOCOL IS DESCRIBED IN DETAIL IN THE MAIN CITATION ASSOCIATED WITH THIS ENTRY.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 15

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