 |
PDBsum entry 3eee
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
3eee
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Signaling protein
|
|
|
Title:
|
|
Probing the function of heme distortion in the h-nox family
|
|
Structure:
|
|
Methyl-accepting chemotaxis protein. Chain: a, b, c, d. Fragment: h-nox domain, residues 1-188. Engineered: yes. Mutation: yes
|
|
Source:
|
|
Thermoanaerobacter tengcongensis. Organism_taxid: 119072. Gene: tar4. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
Resolution:
|
|
|
2.12Å
|
R-factor:
|
0.207
|
R-free:
|
0.252
|
|
|
Authors:
|
|
C.Olea Jr,E.M.Boon,P.Pellicena,J.Kuriyan,M.A.Marletta
|
|
Key ref:
|
|
C.Olea
et al.
(2008).
Probing the function of heme distortion in the H-NOX family.
Acs Chem Biol,
3,
703-710.
PubMed id:
|
|
|
Date:
|
|
|
04-Sep-08
|
Release date:
|
25-Nov-08
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q8RBX6
(Q8RBX6_CALS4) -
Methyl-accepting chemotaxis protein from Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
|
|
|
|
Seq:
Struc:
|
|
|
|
602 a.a.
188 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Acs Chem Biol
3:703-710
(2008)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Probing the function of heme distortion in the H-NOX family.
|
|
C.Olea,
E.M.Boon,
P.Pellicena,
J.Kuriyan,
M.A.Marletta.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Hemoproteins carry out diverse functions utilizing a wide range of chemical
reactivity while employing the same heme prosthetic group. It is clear from
high-resolution crystal structures and biochemical studies that protein-bound
hemes are not planar and adopt diverse conformations. The crystal structure of
an H-NOX domain from Thermoanaerobacter tengcongensis (Tt H-NOX) contains the
most distorted heme reported to date. In this study, Tt H-NOX was engineered to
adopt a flatter heme by mutating proline 115, a conserved residue in the H-NOX
family, to alanine. Decreasing heme distortion in Tt H-NOX increases affinity
for oxygen and decreases the reduction potential of the heme iron. Additionally,
flattening the heme is associated with significant shifts in the N-terminus of
the protein. These results show a clear link between the heme conformation and
Tt H-NOX structure and demonstrate that heme distortion is an important
determinant for maintaining biochemical properties in H-NOX proteins.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
Z.Dai,
and
E.M.Boon
(2011).
Probing the local electronic and geometric properties of the heme iron center in a H-NOX domain.
|
| |
J Inorg Biochem,
105,
784-792.
|
|
|
|
|
|
|
C.Olea,
M.A.Herzik,
J.Kuriyan,
and
M.A.Marletta
(2010).
Structural insights into the molecular mechanism of H-NOX activation.
|
| |
Protein Sci,
19,
881-887.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
J.M.Beames,
A.J.Hudson,
T.D.Vaden,
and
J.P.Simons
(2010).
Double-resonance spectroscopy of the jet-cooled free base and Cu(II) complex of protoporphyrin IX.
|
| |
Phys Chem Chem Phys,
12,
14076-14081.
|
|
|
|
|
|
|
L.J.Smith,
A.Kahraman,
and
J.M.Thornton
(2010).
Heme proteins--diversity in structural characteristics, function, and folding.
|
| |
Proteins,
78,
2349-2368.
|
|
|
|
|
|
|
M.Ibrahim,
E.R.Derbyshire,
M.A.Marletta,
and
T.G.Spiro
(2010).
Probing soluble guanylate cyclase activation by CO and YC-1 using resonance Raman spectroscopy.
|
| |
Biochemistry,
49,
3815-3823.
|
|
|
|
|
|
|
R.Tran,
E.M.Boon,
M.A.Marletta,
and
R.A.Mathies
(2009).
Resonance Raman spectra of an O2-binding H-NOX domain reveal heme relaxation upon mutation.
|
| |
Biochemistry,
48,
8568-8577.
|
|
|
|
|
|
|
W.K.Erbil,
M.S.Price,
D.E.Wemmer,
and
M.A.Marletta
(2009).
A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation.
|
| |
Proc Natl Acad Sci U S A,
106,
19753-19760.
|
|
|
PDB codes:
|
|
|
|
|
|
|
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
codes are
shown on the right.
|
|
Links
