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Biochemistry Department
University of Otago
P.O. Box 56
710 Cumberland St
Dunedin 9054 , New Zealand
Tel.: +64
3 479-5166
FAX: +64 3 479-7866
e-mail: kurt.krause@stonebow.otago.ac.nz
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Research Interests
Structural biology of infectious diseases, structure-aided
drug design, protein crystallography, x-ray diffraction,
structure and function of enzymes and proteins including
antibiotic targets, redox proteins, nucleases, luciferase,
and bacterial pathogenesis factors.
Recent Publications
U. Strych, H. Huang, K. Krause, and M. Benedik, Characterization
of the Alanine Racemases from Pseudomonas aeruginosa
PAO1, (2000) Current Microbiology, 41: 290-294.
Krause, K. L. and Miller, M. D., Using Electrostatics
to Define the Active Site of Serratia Endonuclease
In Methods in Molecular Biology: Nuclease Methods
and Protocols. Eds. C. Schein, Humana Press, Totowa,
NJ (2001), 160: 249-261.
Strych, U., Penland, R. L., Jimenez, M., Krause, K.L.
and M.J. Benedik, Characterization of the alanine racemases
from two Mycobacteria (2001) FEMS Microbiology Letters,
196: 93-98.
Musher, D. M., Dowell, M.E., Shortridge, V.D., Flamm,
R.K., Jorgensen, J.H., Magueres, P. and K. L. Krause,
Emergence of macrolide resistance during treatment of
pneumococcal pneumonia with azithromycin. (2002) New
England J. Med., 346: 630-631.
Bussiere, D. and K. Krause, Biotechnology and Drug
Discovery: Two years into the new millennium, In Technical
Proceedings of the Second International Conference on
Computational Nanoscience and Nanotechnology, Matthew
Laudon and Bart Romanowicz, eds. Computational Publications,
Cambridge. MA. (2002) pp. 44-49.
Crossnoe, C. R., Germanas, J. P., LeMagueres, P., Mustata,
G. and K. L. Krause, The Crystal Structure of Trichomonas
vaginalis Ferredoxin Provides Insight into Metronidazole
Activation, (2002) J. Mol. Biol. (2002) 318:503-518.
Krause, Kurt L. and Miller, Mitchell D., A new engine
for cleaving nucleic acid, In Structures and Mechanisms:
From Ashes to Enzymes, Gareth R. Eaton, Don C.
Wiley, and Oleg Jardetzky, eds., ACS Symposium Series
Volume 827, Oxford University Press, 2002 pp. 270-293.
Vidakovic M, Crossnoe C, Neidre C, Kim K, Krause KL,
Germanas JP. Reactivity of reduced [2Fe-2S] ferredoxins
parallels host susceptibility towards nitroimidazoles.
Antimicrob Agents and Chemother 2003;47(1):
302–308.
Liu L, Im H, Cegielski M, LeMagueres P, Schultz LW,
Krause KL, Hastings JW. Characterization and Crystallization
of Active Domains of a Novel Luciferase from a Marine
Dinoflagellate. Acta Crystalogr D Biol Crystallogr.
2003;59, 2003, 761-764.
Liu L, Im H, Cegielski M, LeMagueres P, Schultz LW,
Krause KL, Hastings JW. Characterization and Crystallization
of Active Domains of a Novel Luciferase from a Marine
Dinoflagellate. Acta Crystalogr D Biol Crystallogr.
2003;59, 2003, 761-764.
Kim MG, Strych U, Krause KL, Benedik MJ, Kohn H. N(2)-substituted
D,L-cycloserine derivatives: synthesis and evaluation
as alanine racemase inhibitors. The Journal of Antibiotics.
2003;56, 160-168.
Krause KL. Nanotech 2003 - Nanotechnology Conference
and Trade Show. Structure-aided drug design. Idrugs.
2003;6(4):309-311.
Kim MG, Ulrich S, Krause KL, Benedik M, Kohn H. Evaluation
of Amino-substituted Heterocyclic Derivatives as Alanine
Racemase Inhibitors. Medicinal Chemistry Research.
2003;12(3) 130-138.
LeMagueres P, Im H, Dvorak A, Strych U, Benedik M,
Briggs J, Krause KL. Crystal structure at 1.45 Å
resolution of alanine racemase from a pathogenic bacterium,
Pseudomonas aeruginosa, contains both internal
and external aldimine forms. Biochemistry.
2003;42(50):14752-61.
LeMagueres, P, Im, H, Ebalunode, J, Strych, U, Benedik,
MJ, Briggs, JM, Kohn, H and Krause,KL “The 1.9
Å crystal structure of alanine racemase from Mycobacterium
tuberculosis contains a conserved entryway into
the active site”, (2005) published online, http://dx.doi.org/10.1021/bi0486583.
Shelburne, S. A., 3rd, Visnegarwala, F., Adams, C.,
Krause, K. L., Hamill, R. J., and White, A. C., Jr.
(2005) Unusual manifestations of disseminated Histoplasmosis
in patients responding to antiretroviral therapy, Am
J Med 118, 1038-1041.
Chen, C. I., Beck, B.W., Krause, K. Pettitt, B. M.
“Solvent Participation in Serratia marcescens
Endonuclease Complexes” (2005) Proteins: Structure,
Function and Bioinformatics, 62 (4): 982-99.
Hastings, J.W. and Krause, K. L., “Luciferases
and Light Emitting Accessory Proteins: Structural Biology”
(2006) Nature Encyclopedia of Life Sciences,
John Wiley & Sons, Ltd: Chichester http://www.els.net/ [doi:10.1038/npg.els.0003064].
Chen, C. I., Beck, B.W., Krause, K., Weksberg, T. E., Pettitt, B. M. “Effects of dimerization of Serratia marcescens endonuclease on water dynamics” (2007) Biopolymers, 85 (3): 241-252.
Weksberg, T. E., Lynch, G. C., , Krause, K. L., Pettitt, B. M. “Molecular Dynamics Simulations of Trichomonas vaginalis Ferredoxin Show Loop-Cap Transition” (2007) Biophysical J., 92: 3337-3345.
Ulrich Strych, Milya Davlieva, Joseph P. Longtin, Eileen L. Murphy, Hookang Im, Michael J. Benedik, and Kurt L. Krause, “Purification and preliminary crystallization of alanine racemase from Streptococcus pneumoniae ” (2007) BMC Microbiology, 7:40 (17 May 2007).
Daniel L. Milligan, Sieu L. Tran, Ulrich Strych, Gregory M. Cook, and Kurt L. Krause, “The Alanine Racemase of Mycobacterium smegmatis is Essential for Growth in the Absence of D-Alanine” J. Bacteriol. 189 (22) 8381-8386. (Published ahead of print on 7 September 2007, doi:10.1128/JB.01201-07)
Chuanying Chen, Kurt Krause, B Pettitt . (2008) Advantage of Being a Dimer for Serratia marcescens Endonuclease, J. Physical Chemistry B, 2009, 113(2), 511-521. (Cover Art)
Rafael M Couñago, Milya Davlieva, Ulrich Strych, Ryan E Hill, and Kurt L Krause (2009) Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames), BMC Structural Biology 2009, 9(53) (20 August 2009)
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