Interdisciplinary Life Science - PULSe Great research is a matter of choice

Nicholas Noinaj

Nicholas Noinaj Profile Picture

Postdoc, NIDDK/NIH
PhD, Biochemistry, University of Kentucky
BA/BA, Chemistry/Mathematics, Berea College


Contact Info:

nnoinaj@purdue.edu


Training Group(s):
Biomolecular Structure and Biophysics
Membrane Biology


Current Research Interests:

My research interests are in understanding how pathogenic Gram-negative bacteria are able to use virulence factors found on their surface to mediate infection.  These virulence factors are found in the outer membrane and belong to a class of surface proteins commonly referred to as outer membrane proteins (OMPs).  In particular, my lab will investigate the multi-component complex called the BAM complex, which is responsible for the biogenesis of all OMPs, in hopes of understanding how it is able to fold and insert OMPs into the outer membrane.  We will use a combination of techniques to accomplish this including X-ray crystallography, electron microscopy, crosslinking, and various functional assays.  Our ultimate goal is to use the information from the structural and functional characterization as a starting point for drug discovery and development targeting the BAM complex in a species specific manner.



Selected Publications:

O’ Neil P, Richardson LGL, Paila YD, Piszczek G, Chakravarthy S, Noinaj N*, Schnell DJ*. The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts. PNAS. 2017, (in press).

Noinaj N, Gumbart JC, Buchanan SK. The β-barrel assembly machinery in motion. Nat Rev Microbiol 2017, 15(4):197-204. (Cover Image)

Bakelar J, Buchanan SK, Noinaj N. Structural snapshots of the β-barrel assembly machinery. FEBS J 2016, doi: 10.1111/febs.13960.

Celia H, Noinaj N*, Zakharov SD, Bordignon E, Botos I, Santamaria M, Barnard TJ, Cramer WA, Lloubes R*, Buchanan SK*. Structural insight into the role of the Ton complex in energy transduction. Nature 2016, 538(7623):60-65.

Bakelar J, Buchanan SK, Noinaj N. The structure of the β-barrel assembly machinery complex. Science 2016, 351(6269):180-6.

O'Neil PK, Rollauer SE, Noinaj N, Buchanan SK. Fitting the pieces of the β-barrel assembly machinery complex. Biochemistry 2015, 54(41):6303-11.

Noinaj N, Kuszak AJ, Balusek C, Gumbart JC, Buchanan SK. Lateral opening and exit pore formation are required for BamA function. Structure 2014, 22(7):1055-62.

Noinaj N, Kuszak AJ, Gumbart JC, Lukacik P, Chang H, Easley NC, Lithgow T, Buchanan SK. Structural insight into the biogenesis of β-barrel membrane proteins. Nature 2013, 501(7467):385-90.

Noinaj N, Cornelissen CN, Buchanan SK. Structural insight into the lactoferrin receptors from pathogenic Neisseria. J. Structural Biology 2013, 184(1):83-92.

White JF, Noinaj N, Shibata Y, Love J, Kloss B, Xu F, Gvozdenovic-Jeremic J, Shah P, Shiloach J, Tate CG, Grisshammer R. Structure of the agonist-bound neurotensin receptor. Nature 2012, 490(7421):508-13.

Noinaj N, Buchanan SK, Cornelissen CN. The transferrin-iron import system from pathogenic Neisseria species. Mol Microbiol. 2012, 86(2):246-57.

Noinaj N, Easley NC, Oke M, Mizuno N, Gumbart J, Boura E, Steere AN, Zak O, Aisen P, Tajkhorshid E, Evans RW, Gorringe AR, Mason AB, Steven AC, Buchanan SK. Structural basis for iron piracy by pathogenic Neisseria. Nature 2012, 483(7387):53-8.

Noinaj N, Bosserman MA, Schickli MA, Piszczek G, Kharel MK, Pahari P, Buchanan SK, Rohr J. The crystal structure and mechanism of an unusual oxidoreductase, GilR, involved in gilvocarcin V biosynthesis. J Biol Chem. 2011 286(26):23533-43.

Noinaj N, Fairman JW, Buchanan SK. The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex. J Mol Biol. 2011 Mar 25;407(2):248-60.

Noinaj N, Guillier M, Barnard TJ, Buchanan SK. TonB-dependent transporters: regulation, structure, and function. Annu Rev Microbiol. 2010, 64:43-60.

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