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PDBsum entry 1pl3

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
1pl3
Jmol
Contents
Protein chains
186 a.a. *
Ligands
NAG-NAG ×2
HEM ×2
1PG
Metals
_CD ×6
Waters ×336
* Residue conservation analysis
PDB id:
1pl3
Name: Oxidoreductase
Title: Cytochrome domain of cellobiose dehydrogenase, m65h mutant
Structure: Cellobiose dehydrogenase. Chain: a, b. Fragment: cytochrome type b heme domain. Synonym: cdh, cellobiose-quinone oxidoreductase. Engineered: yes. Mutation: yes
Source: Phanerochaete chrysosporium. Organism_taxid: 5306. Gene: cdh-1 and cdh-2. Expressed in: phanerochaete chrysosporium. Expression_system_taxid: 5306.
Resolution:
1.90Å     R-factor:   0.174     R-free:   0.198
Authors: F.A.J.Rotsaert,B.M.Hallberg,S.De Vries,P.Moenne-Loccoz,C.Div M.H.Gold
Key ref:
F.A.Rotsaert et al. (2003). Biophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenase. J Biol Chem, 278, 33224-33231. PubMed id: 12796496 DOI: 10.1074/jbc.M302653200
Date:
06-Jun-03     Release date:   01-Jul-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q01738  (CDH_PHACH) -  Cellobiose dehydrogenase
Seq:
Struc:
 
Seq:
Struc:
773 a.a.
186 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.1.1.99.18  - Cellobiose dehydrogenase (acceptor).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor
Cellobiose
+ acceptor
= cellobiono-1,5-lactone
+ reduced acceptor
      Cofactor: FAD; Heme
FAD
Heme
Bound ligand (Het Group name = HEM) matches with 95.45% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M302653200 J Biol Chem 278:33224-33231 (2003)
PubMed id: 12796496  
 
 
Biophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenase.
F.A.Rotsaert, B.M.Hallberg, S.de Vries, P.Moenne-Loccoz, C.Divne, V.Renganathan, M.H.Gold.
 
  ABSTRACT  
 
The fungal extracellular flavocytochrome cellobiose dehydrogenase (CDH) participates in lignocellulose degradation. The enzyme has a cytochrome domain connected to a flavin-binding domain by a peptide linker. The cytochrome domain contains a 6-coordinate low spin b-type heme with unusual iron ligands and coordination geometry. Wild type CDH is only the second example of a b-type heme with Met-His ligation, and it is the first example of a Met-His ligation of heme b where the ligands are arranged in a nearly perpendicular orientation. To investigate the ligation further, Met65 was replaced with a histidine to create a bis-histidyl ligated iron typical of b-type cytochromes. The variant is expressed as a stable 90-kDa protein that retains the flavin domain catalytic reactivity. However, the ability of the mutant to reduce external one-electron acceptors such as cytochrome c is impaired. Electrochemical measurements demonstrate a decrease in the redox midpoint potential of the heme by 210 mV. In contrast to the wild type enzyme, the ferric state of the protoheme displays a mixed low spin/high spin state at room temperature and low spin character at 90 K, as determined by resonance Raman spectroscopy. The wild type cytochrome does not bind CO, but the ferrous state of the variant forms a CO complex, although the association rate is very low. The crystal structure of the M65H cytochrome domain has been determined at 1.9 A resolution. The variant structure confirms a bis-histidyl ligation but reveals unusual features. As for the wild type enzyme, the ligands have a nearly perpendicular arrangement. Furthermore, the iron is bound by imidazole N delta 1 and N epsilon 2 nitrogen atoms, rather than the typical N epsilon 2/N epsilon 2 coordination encountered in bis-histidyl ligated heme proteins. To our knowledge, this is the first example of a bis-histidyl N delta 1/N epsilon 2-coordinated protoporphyrin IX iron.
 
  Selected figure(s)  
 
Figure 3.
FIG. 3. High frequency RR spectra of the oxidized rCDH and the M65H variant, obtained at room temperature (RT, A) and 90 K(B), with Soret excitation (413 nm) in 20 mM sodium succinate, pH 4.5.
Figure 5.
FIG. 5. a, the [A]-weighted F[o] - F[c] electron density around the iron-protoporphyrin IX ring in the M65H cytochrome domain. The 6-coordinate heme iron is ligated by His65 N 1 and His163 N 2. b, superposition of the M65H variant (gold) and wild type (green) heme-binding pocket (Protein Data Bank code 1D7C [PDB] ) (7). The drawings were made with the program Pymol (pymol.sourceforge.net).
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 33224-33231) copyright 2003.  
  Figures were selected by an automated process.