 |
PDBsum entry 1ilo
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Structural genomics
|
PDB id
|
|
|
|
1ilo
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Identification of a novel archaebacterial thioredoxin: determination of function through structure.
|
|
|
Authors
|
|
S.Bhattacharyya,
B.Habibi-Nazhad,
G.Amegbey,
C.M.Slupsky,
A.Yee,
C.Arrowsmith,
D.S.Wishart.
|
|
|
Ref.
|
|
Biochemistry, 2002,
41,
4760-4770.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
79%.
|
|
|
|
Abstract
|
|
|
As part of a high-throughput, structural proteomic project we have used NMR
spectroscopy to determine the solution structure and ascertain the function of a
previously unknown, conserved protein (MtH895) from the thermophilic archeon
Methanobacterium thermoautotrophicum. Our findings indicate that MtH895 contains
a central four-stranded beta-sheet core surrounded by two helices on one side
and a third on the other. It has an overall fold superficially similar to that
of a glutaredoxin. However, detailed analysis of its three-dimensional structure
along with molecular docking simulations of its interaction with T7 DNA
polymerase (a thioredoxin-specific substrate) and comparisons with other known
members of the thioredoxin/glutaredoxin family of proteins strongly suggest that
MtH895 is more akin to a thioredoxin. Furthermore, measurement of the pK(a)
values of its active site thiols along with direct measurements of the
thioredoxin/glutaredoxin activity has confirmed that MtH895 is, indeed, a
thioredoxin and exhibits no glutaredoxin activity. We have also identified a
group of previously unknown proteins from several other archaebacteria that have
significant (34-44%) sequence identity with MtH895. These proteins have unusual
active site -CXXC- motifs not found in any known thioredoxin or glutaredoxin. On
the basis of the results presented here, we predict that these small proteins
are all members of a new class of truncated thioredoxins.
|
|
|
|
|
|
|
