PDBsum entry 1ft6

Electron transport

PDB id

1ft6

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Contents

			Protein chain

					208 a.a. *

			Ligands

					SO3


					PO4


					HEC ×4


					DTN

			Waters ×142

* Residue conservation analysis

PDB id:

1ft6

Links

Name:

Electron transport

Title:

Reduced state of cytochrome c554 from nitrosomonas europaea

Structure:

Cytochrome c554. Chain: a. Synonym: c554, hydroxylamine oxidoreductase-linked cytochrome

Source:

Nitrosomonas europaea. Organism_taxid: 915

Resolution:

1.80Å

R-factor:

0.197

R-free:

0.236

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

	Headers

	References

Protein chain

Q57142 (C554_NITEU) - Cytochrome c-554 from Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)

Seq: Struc:					235 a.a. 208 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.