PDBsum entry 2khr

Biosynthetic protein

PDB id: 2khr

Contents

Protein chain

74 a.a. *

* Residue conservation analysis

PDB id:

2khr

Name:

Biosynthetic protein

Title:

Solution structure of rv2377c, a mbth-like protein from mycobacterium tuberculosis

Structure:

Protein mbth. Chain: a. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: mbth, mt2445.1, mtcy27.03, rv2377c. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

G.W.Buchko,C.Y.Kim,T.C.Terwilliger,Seattle Structural Genomics Center For Infectious Disease (Ssgcid)

Key ref:

G.W.Buchko et al. (2010). Solution structure of Rv2377c-founding member of the MbtH-like protein family. Tuberculosis (edinb), 90, 245-251. PubMed id: 20434955

Date:

10-Apr-09 Release date: 05-May-09

Protein chain

P9WIP5  (MBTH_MYCTU) -  Protein MbtH from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: 71 a.a.

Struc: 74 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Tuberculosis (edinb) 90:245-251 (2010)

PubMed id: 20434955

Solution structure of Rv2377c-founding member of the MbtH-like protein family.

G.W.Buchko, C.Y.Kim, T.C.Terwilliger, P.J.Myler.

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.