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Structural, bioinformatic, and in vivo analyses of two Treponema pallidum lipoproteins reveal a unique TRAP transporter.

Deka RK, Brautigam CA, Goldberg M, Schuck P, Tomchick DR, Norgard MV.

J Mol Biol. 2012 Mar 9;416(5):678-96. doi: 10.1016/j.jmb.2012.01.015. Epub 2012 Jan 27.


Structural and thermodynamic characterization of the interaction between two periplasmic Treponema pallidum lipoproteins that are components of a TPR-protein-associated TRAP transporter (TPAT).

Brautigam CA, Deka RK, Schuck P, Tomchick DR, Norgard MV.

J Mol Biol. 2012 Jun 29;420(1-2):70-86. doi: 10.1016/j.jmb.2012.04.001. Epub 2012 Apr 11.


The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum.

Deka RK, Brautigam CA, Yang XF, Blevins JS, Machius M, Tomchick DR, Norgard MV.

J Biol Chem. 2006 Mar 24;281(12):8072-81. Epub 2006 Jan 16.


Biophysical and bioinformatic analyses implicate the Treponema pallidum Tp34 lipoprotein (Tp0971) in transition metal homeostasis.

Brautigam CA, Deka RK, Ouyang Z, Machius M, Knutsen G, Tomchick DR, Norgard MV.

J Bacteriol. 2012 Dec;194(24):6771-81. doi: 10.1128/JB.01494-12. Epub 2012 Oct 5.


Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an L-methionine-binding protein.

Deka RK, Neil L, Hagman KE, Machius M, Tomchick DR, Brautigam CA, Norgard MV.

J Biol Chem. 2004 Dec 31;279(53):55644-50. Epub 2004 Oct 15.


Structural and biochemical basis for polyamine binding to the Tp0655 lipoprotein of Treponema pallidum: putative role for Tp0655 (TpPotD) as a polyamine receptor.

Machius M, Brautigam CA, Tomchick DR, Ward P, Otwinowski Z, Blevins JS, Deka RK, Norgard MV.

J Mol Biol. 2007 Oct 26;373(3):681-94. Epub 2007 Aug 21.


Tripartite ATP-independent Periplasmic (TRAP) Transporters Use an Arginine-mediated Selectivity Filter for High Affinity Substrate Binding.

Fischer M, Hopkins AP, Severi E, Hawkhead J, Bawdon D, Watts AG, Hubbard RE, Thomas GH.

J Biol Chem. 2015 Nov 6;290(45):27113-23. doi: 10.1074/jbc.M115.656603. Epub 2015 Sep 5.


Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport.

Cuneo MJ, Changela A, Miklos AE, Beese LS, Krueger JK, Hellinga HW.

J Biol Chem. 2008 Nov 21;283(47):32812-20. doi: 10.1074/jbc.M803595200. Epub 2008 Aug 22.


Crystal structure of the Tp34 (TP0971) lipoprotein of treponema pallidum: implications of its metal-bound state and affinity for human lactoferrin.

Deka RK, Brautigam CA, Tomson FL, Lumpkins SB, Tomchick DR, Machius M, Norgard MV.

J Biol Chem. 2007 Feb 23;282(8):5944-58. Epub 2006 Dec 27.


Crystal structure of a periplasmic substrate-binding protein in complex with calcium lactate.

Akiyama N, Takeda K, Miki K.

J Mol Biol. 2009 Sep 25;392(3):559-65. doi: 10.1016/j.jmb.2009.07.043. Epub 2009 Jul 22.


Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA.

Vergauwen B, Elegheert J, Dansercoer A, Devreese B, Savvides SN.

Proc Natl Acad Sci U S A. 2010 Jul 27;107(30):13270-5. doi: 10.1073/pnas.1005198107. Epub 2010 Jul 13.


The general transition metal (Tro) and Zn2+ (Znu) transporters in Treponema pallidum: analysis of metal specificities and expression profiles.

Desrosiers DC, Sun YC, Zaidi AA, Eggers CH, Cox DL, Radolf JD.

Mol Microbiol. 2007 Jul;65(1):137-52.


Periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE.

Jacso T, Grote M, Daus ML, Schmieder P, Keller S, Schneider E, Reif B.

Biochemistry. 2009 Mar 17;48(10):2216-25. doi: 10.1021/bi801376m.


Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump.

Yum S, Xu Y, Piao S, Sim SH, Kim HM, Jo WS, Kim KJ, Kweon HS, Jeong MH, Jeon H, Lee K, Ha NC.

J Mol Biol. 2009 Apr 17;387(5):1286-97. doi: 10.1016/j.jmb.2009.02.048. Epub 2009 Feb 28.


Evidence for an ABC-type riboflavin transporter system in pathogenic spirochetes.

Deka RK, Brautigam CA, Biddy BA, Liu WZ, Norgard MV.

MBio. 2013 Feb 12;4(1):e00615-12. doi: 10.1128/mBio.00615-12.


The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent transcriptional repressor, and a semi-autonomously expressed phosphoglycerate mutase.

Hazlett KR, Rusnak F, Kehres DG, Bearden SW, La Vake CJ, La Vake ME, Maguire ME, Perry RD, Radolf JD.

J Biol Chem. 2003 Jun 6;278(23):20687-94. Epub 2003 Mar 31.


Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone.

Lee YH, Deka RK, Norgard MV, Radolf JD, Hasemann CA.

Nat Struct Biol. 1999 Jul;6(7):628-33.


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