2KHR

Solution structure of Rv2377c, a MbtH-like protein from Mycobacterium tuberculosis

Summary for 2KHR

• Entry DOI: 10.2210/pdb2khr/pdb
• NMR Information: BMRB: 16253
• Descriptor: Protein mbtH (1 entity in total)
• Functional Keywords: siderophores, mycobactin, mtbh-like, 2-hydroxyphenyloxazoline, tuberculosis, biosynthetic protein, structural genomics, seattle structural genomics center for infectious disease, ssgcid
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 8372.17

Authors

Buchko, G.W.,Kim, C.Y.,Terwilliger, T.C.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2009-04-10, release date: 2009-05-05, Last modification date: 2024-05-08)

Primary citation

Buchko, G.W.,Kim, C.Y.,Terwilliger, T.C.,Myler, P.J.
Solution structure of Rv2377c-founding member of the MbtH-like protein family.
Tuberculosis (Edinb), 90:245-251, 2010

PubMed Abstract: The Mycobacterium tuberculosis protein Rv2377c (71 residues, MW=8.4kDa) has been characterized using nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. Rv2377c was the first identified member of the MbtH-like family of proteins. MbtH-like proteins have been implicated in siderophore biosynthesis, however, their precise biochemical function remain unknown. Size exclusion chromatography and NMR spectroscopy show that Rv2377c is a monomer in solution. Circular dichroism spectroscopy indicates that Rv2377c unfolds upon heating and will reversibly fold into its native conformation upon cooling. Using NMR-based methods the solution structure of Rv2377c was determined and some of the dynamic properties of the protein studied. The protein contains a three-strand, anti-parallel beta-sheet (beta3:beta1:beta2) nestled against one C-terminal alpha-helix (S44-N55). Weak or absent amide cross peaks in the (1)H-(15)N HSQC spectrum for many of the beta1 and beta2 residues suggest intermediate motion on the ms to mus time scale at the beta1:beta2 interface. Amide cross peaks in the (1)H-(15)N HSQC spectrum are absent for all but one residue at the C-terminus (W56-D71), a region that includes a highly conserved sequence WXDXR, suggesting this region is intrinsically disordered. The latter observation differs with the crystal structure of another MbtH-like protein, PA2412 from Pseudomonas aeruginosa, where a second ordered alpha-helix was observed at the extreme C-terminus.

PubMed: 20434955
DOI: 10.1016/j.tube.2010.04.002

Experimental method

SOLUTION NMR