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PDBsum entry 1ft5
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Electron transport PDB id
1ft5

 

 

 

 

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Contents
Protein chain
211 a.a. *
Ligands
PO4 ×3
HEM ×4
Waters ×142
* Residue conservation analysis
PDB id:
1ft5
Name: Electron transport
Title: Crystal structure of the oxidized state of cytochrome c554 from nitrosomonas europaea
Structure: Cytochrome c554. Chain: a. Synonym: c554, hydroxylamine oxidoreductase-linked cytochrome
Source: Nitrosomonas europaea. Organism_taxid: 915. Other_details: chemoautotrophic bacterium involved in biological nitrification
Resolution:
1.60Å     R-factor:   0.188     R-free:   0.215
Authors: T.M.Iverson,D.M.Arciero,A.B.Hooper,D.C.Rees
Key ref: T.M.Iverson et al. (2001). High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea. J Biol Inorg Chem, 6, 390-397. PubMed id: 11372197
Date:
11-Sep-00     Release date:   20-Sep-00    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q57142  (C554_NITEU) -  Cytochrome c-554 from Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
Seq:
Struc: 		235 a.a.
211 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
J Biol Inorg Chem 6:390-397 (2001)
PubMed id: 11372197  
 
 
High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea.
T.M.Iverson, D.M.Arciero, A.B.Hooper, D.C.Rees.
 
  ABSTRACT  
 
Cytochrome c554 (cyt c554) is a tetra-heme cytochrome involved in the oxidation of NH3 by Nitrosomonas europaea. The X-ray crystal structures of both the oxidized and dithionite-reduced states of cyt c554 in a new, rhombohedral crystal form have been solved by molecular replacement, at 1.6 A and 1.8 A resolution, respectively. Upon reduction, the conformation of the polypeptide chain changes between residues 175 and 179, which are adjacent to hemes III and IV. Cyt c554 displays conserved heme-packing motifs that are present in other heme-containing proteins. Comparisons to hydroxylamine oxidoreductase, the electron donor to cyt c554, and cytochrome c nitrite reductase, an enzyme involved in nitrite ammonification, reveal substantial structural similarity in the polypeptide chain surrounding the heme core environment. The structural determinants of these heme-packing motifs extend to the buried water molecules that hydrogen bond to the histidine ligands to the heme iron. In the original structure determination of a tetragonal crystal form, a cis peptide bond between His129 and Phe130 was identified that appeared to be stabilized by crystal contacts. In the rhombohedral crystal form used in the present high-resolution structure determination, this peptide bond adopts the trans conformation, but with disallowed angles of phi and psi.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20544970 L.J.Smith, A.Kahraman, and J.M.Thornton (2010).
Heme proteins--diversity in structural characteristics, function, and folding.
  Proteins, 78, 2349-2368.  
18505274 H.J.Kim, A.Zatsman, A.K.Upadhyay, M.Whittaker, D.Bergmann, M.P.Hendrich, and A.B.Hooper (2008).
Membrane tetraheme cytochrome c(m552) of the ammonia-oxidizing nitrosomonas europaea: a ubiquinone reductase.
  Biochemistry, 47, 6539-6551.  
18553112 J.Kostera, M.D.Youngblut, J.M.Slosarczyk, and A.A.Pacheco (2008).
Kinetic and product distribution analysis of NO* reductase activity in Nitrosomonas europaea hydroxylamine oxidoreductase.
  J Biol Inorg Chem, 13, 1073-1083.  
18031536 M.G.Klotz, and L.Y.Stein (2008).
Nitrifier genomics and evolution of the nitrogen cycle.
  FEMS Microbiol Lett, 278, 146-156.  
16569009 A.K.Upadhyay, A.B.Hooper, and M.P.Hendrich (2006).
NO reductase activity of the tetraheme cytochrome C554 of Nitrosomonas europaea.
  J Am Chem Soc, 128, 4330-4337.  
16234915 C.G.Mowat, and S.K.Chapman (2005).
Multi-heme cytochromes--new structures, new chemistry.
  Dalton Trans, (), 3381-3389.  
16151127 D.J.Bergmann, A.B.Hooper, and M.G.Klotz (2005).
Structure and sequence conservation of hao cluster genes of autotrophic ammonia-oxidizing bacteria: evidence for their evolutionary history.
  Appl Environ Microbiol, 71, 5371-5382.  
12657783 D.Aragão, C.Frazão, L.Sieker, G.M.Sheldrick, J.LeGall, and M.A.Carrondo (2003).
Structure of dimeric cytochrome c3 from Desulfovibrio gigas at 1.2 A resolution.
  Acta Crystallogr D Biol Crystallogr, 59, 644-653.
PDB code: 1gyo
12796496 F.A.Rotsaert, B.M.Hallberg, S.de Vries, P.Moenne-Loccoz, C.Divne, V.Renganathan, and M.H.Gold (2003).
Biophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenase.
  J Biol Chem, 278, 33224-33231.
PDB code: 1pl3
12423372 I.J.Correia, C.M.Paquete, R.O.Louro, T.Catarino, D.L.Turner, and A.V.Xavier (2002).
Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans.
  Eur J Biochem, 269, 5722-5730.  
11551953 R.O.Louro, I.Bento, P.M.Matias, T.Catarino, A.M.Baptista, C.M.Soares, M.A.Carrondo, D.L.Turner, and A.V.Xavier (2001).
Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome.
  J Biol Chem, 276, 44044-44051.
PDB codes: 1gm4 1gmb
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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