Anders Bergkvist - CV
Curriculum Vitae of Anders Bergkvist
Born 23rd of November 1969 in Skara, Sweden
Swedish citizen
Married, no children
Education
January 1996: Master of Engineering Physics at
Chalmers University of Technology, Göteborg, Sweden
expected in September 2000: Ph.D. on "Structural Studies on
Plastocyanin and Transhydrogenase by NMR"
Extra curricular activities at Chalmers
1992-93: President of Chalmers Aerospace Club
1993: Participation in BEST summer course in Grenoble, France
1994: COMETT-scholarship for research practice in Lisbon, Portugal
Research activities
Plastocyanin (one manuscript submitted, two more to come)
Structure, dynamics and interaction with cytochrome f
Transhydrogenase (two accepted papers, two more to come)
Assignments and global fold of domain III, domain and substrate interactions
Azurin (one or two papers to come)
Structure
Universal stress protein A, uspA
Assignments, phosphorylation site, structure, function, ...
References
Prof. Martin Billeter email: martin.billeter@bcbp.gu.se tfn: +46 31 7733925
address: Dept. of Biochemistry and Biophysics, Göteborg University
Docent Göran Karlsson email: goran.karlsson@bcbp.chalmers.se tfn: +46 31 7733917
address: Dept. of Molecular Biotechnology, Chalmers University of Technology
Prof. Thomas Nyström email: thomas.nystrom@gmm.gu.se tfn: +46 31 7732582
address: Dept. of Cell and Molecular Biology - Microbiology, Göteborg University
Lundberglab, P.O. Box 462, S-405 30 Göteborg, Sweden (applies to all)
Plastocyanin
This was my original project, started in 1995. The main issue is to determine
a high-resolution structure of spinach plastocyanin. Due to several different
problems, this project has been somewhat delayed.
There are already several X-ray and NMR structures of plastocyanin from other
species; specifically, there are very nice NMR structures of parsley and french
bean. We therefore realized, a year or so into the project, that a structure of
spinach plastocyanin would not bring substantially new information to the field
and that we should expand our project to include NMR relaxation analyses as
well, before publication.
Later, our structure was also used in interaction studies between pc and cytf
and that will also be a part of my thesis work.
Publications in prepation:
"High-resolution Solution Structure and 15N-relaxation
Analysis of Spinach Plastocyanin", A Bergkvist,
S Young and B G Karlsson. Will be submitted to Biochemistry during spring of
2000.
"Side-chain Interactions in the Plastocyanin-Cytochrome f Complex
as Determined by 1H-NMR Chemical-shift Analysis",
M Ejdebäck, A Bergkvist, G W Canters, B G Karlsson and M Ubbink.
Will be submitted to Biochemistry this or next week.
"Side-chain Interactions in the E43Q/D44N and E59K/E60Q Plastocyanin
double-mutants to Cytochrome f Complex as Determined by
1H-NMR Chemical-shift Analysis", A Bergkvist,
M Ejdebäck, B G Karlsson and M Ubbink. Will be submitted during spring
of 2000.
Related publication:
"The structure of the complex of plastocyanin and cytochrome f,
determined by paramagnetic NMR and restrained rigid-body molecular
dynamics", M Ubbink, M Ejdebäck, B G Karlsson and D S Bendall,
Structure 6 (1998), 323-335
Transhydrogenase
This project was started in 1997 in cooperation with Prof. Jan Rydström
and coworkers. Transhydrogenase is a membrane-bound enzyme that couples the
reversible reduction of NADP+ by NADH to a proton translocation
across the cytoplasmic membrane. The protein is composed of three domains, the
NAD(H)-binding domain I, the membrane-spanning domain II and the
NADP(H)-binding domain III.
We have cloned and expressed both soluble domains of E. coli
transhydrogenase, ecI (dimer of 2´42.8 kDa)
and ecIII (monomer of 20.4 kDa). We have published an essentially complete
backbone assignment of ecIII and we also have a publication on its global
fold and substrate-binding site. Currently we are working on interaction
studies between ecIII and ecI, and the application of residual dipolar
couplings for the structure determination of ecIII.
Existing publications:
"Sequential assignment and secondary structure analysis of the
NADP(H)-binding domain of Escherichia coli transhydrogenase",
C Johansson, A Bergkvist, O Fjellström, J Rydström and
B G Karlsson, J. Biomol. NMR 14 (1999), 295-296.
"NMR Characterization of the NADP(H)-binding Domain of Eschericia
coli Transhydrogenase; Sequential Assignment and Global Fold",
C Johansson, A Bergkvist, O Fjellström, J Rydström and
B G Karlsson, FEBS Lett. 458 (1999), 180-184.
Publications in prepation:
"Domain Interactions in Transhydrogenase studied by NMR and
Mutagenesis", A Bergkvist, C Johansson, T Johansson,
JRydström and B G Karlsson. Will be submitted to Biochemistry
during autumn of 1999.
"Residual Dipolar Coupling Measurements in the NADP(H)-binding domain of
Escherichia coli transhydrogenase", A Bergkvist,
T Papavoine, T Johansson, M Billeter and B G Karlsson. Will be submitted
during spring of 2000.
Azurin
Like plastocyanin this is a protein which was available at the department
when I started my graduate studies. There are also several X-ray structures
available of this protein, but as of yet there is no NMR structure. This is
not my main project and it will not be included in my dissertation thesis,
but I have been involved with it during the course of the project and I expect
to continue playing an advisory role here.
Publications in prepation:
"Sequential Assignment of Pseudomonas Aeruginosa Azurin",
J Leckner, A Bergkvist and BG Karlsson. Estimated to be submitted during
spring of 2000.
"High-resolution Solution Structure of Pseudomonas Aeruginosa
Azurin", J Leckner, A Bergkvist and B G Karlsson. Estimated to be
submitted during autumn of 2000.
Universal Stress Protein A (UspA)
This project is a rather new NMR project and it is done in cooperation with
Prof. Thomas Nyström. The major NMR work that has been done so far has
been done by a diploma worker under my supervision.
UspA is an E. coli protein (15.9 kDa) which is transcriptionally
induced, when the cell reaches stasis, as a function of various stress factors.
The protein has been cloned and overexpresses all right in rich as well as in
minimal medium (>7 mg/l). We have an (more than two years) old sample grown
on rich medium which show no deterioration. However, we have had some problem
with stability on proteins grown in minimal medium. A possible explanation of
this is a problem with some purification step. Despite this, presumably
transient, problem, we have been able to detect 15N-HSQC spectra
(before the protein deteriorated) which show signal dispersion indicative of a
defined fold. We also know that the protein is a dimer (total weight of 32 kDa)
and that it is overexpressed with one phosphate attached to each monomer, in
rich medium.
In my mind, devising a purification procedure that will leave a stable protein
also in minimal medium shouldn’t be too difficult. After that, a backbone
assignment would require 15N- and 13C-labeling and
possibly 2H-labeling. However, a backbone assignment would then
enable identification of not only secondary structure elements but also of the
phosphorylation site as well as a possible ATP-binding site. Further side-chain
assignments and structure calculations would require special attention to the
dimeric form of the protein, but would still be quite possible.
The structure of uspA would be very interesting since no sequence homologies
have been found to existing structures. The structure would also be very
interesting since the protein have a well-characterized physiological, but not
biochemical, function.
Related publications:
"Cloning, mapping and nucleotide sequencing of a gene encoding a universal
stress protein in Escherichia coli", T Nyström and
F C Neidhardt, Mol. Microbiol. 6 (1992), 3187-3198
"The Universal Stress Protein, UspA, of Escherichia coli is
Phosphorylated in Response to Stasis", Freestone et al., J. Mol. Biol.
274 (1997), 318-324