Mycobacterium tuberculosis ArfA Rv0899
From Proteopedia
(Difference between revisions)
| Line 21: | Line 21: | ||
The C domain <scene name='61/612805/C_domain/1'>(residues 201-326)</scene> has homology to the OmpA-C-like superfamily of periplasmic peptidoglycan-binding sequences, found in several types of bacterial membrane proteins.The C domain of wild-type ArfA folds into four β-strands and four α-helices, arranged in the topological order αβαβαβαβ (Fig. 1a). Three parallel (β1, β2, β3) and one antiparallel (β4) β-strands form a four-stranded β-sheet (β1–β4-β2–β3) that packs against three α-helices (α1, α2, α3), while a fourth helix (α4) extends from the N-terminus of β4. A disulfide bond between C208 and C250 connects the N-terminus of α1 to the C-terminus of α2.<ref>PMID: 20199110</ref> | The C domain <scene name='61/612805/C_domain/1'>(residues 201-326)</scene> has homology to the OmpA-C-like superfamily of periplasmic peptidoglycan-binding sequences, found in several types of bacterial membrane proteins.The C domain of wild-type ArfA folds into four β-strands and four α-helices, arranged in the topological order αβαβαβαβ (Fig. 1a). Three parallel (β1, β2, β3) and one antiparallel (β4) β-strands form a four-stranded β-sheet (β1–β4-β2–β3) that packs against three α-helices (α1, α2, α3), while a fourth helix (α4) extends from the N-terminus of β4. A disulfide bond between C208 and C250 connects the N-terminus of α1 to the C-terminus of α2.<ref>PMID: 20199110</ref> | ||
| - | = Function== | + | ==Function== |
The membrane protein Rv0899 ArfA belongs to the OmpA (outer membrane protein A) family of outer membrane proteins and has been proposed to act as an outer membrane [[porin]] and to contribute to the bacterium's adaptation to the acidic environment of the phagosome[http://en.wikipedia.org/wiki/Phagosome] during infection.The deletion of this gene impairs the uptake of some water-soluble substances, such as serine, glucose, and glycerol. | The membrane protein Rv0899 ArfA belongs to the OmpA (outer membrane protein A) family of outer membrane proteins and has been proposed to act as an outer membrane [[porin]] and to contribute to the bacterium's adaptation to the acidic environment of the phagosome[http://en.wikipedia.org/wiki/Phagosome] during infection.The deletion of this gene impairs the uptake of some water-soluble substances, such as serine, glucose, and glycerol. | ||
Using [[NMR]] chemical shift perturbation and isothermal calorimetric titration assays, Rv0899 was able to interact with <scene name='61/612805/Binding-site_for_zn/1'>Zn(2+) ions</scene>, which may indicate a role for Rv0899 in the process of Zn(2+) acquisition. | Using [[NMR]] chemical shift perturbation and isothermal calorimetric titration assays, Rv0899 was able to interact with <scene name='61/612805/Binding-site_for_zn/1'>Zn(2+) ions</scene>, which may indicate a role for Rv0899 in the process of Zn(2+) acquisition. | ||
Revision as of 15:12, 17 January 2015
| |||||||||||
