Mycobacterium tuberculosis ArfA Rv0899
From Proteopedia
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==Structure Section== | ==Structure Section== | ||
| - | The 326-residue Rv0899 ArfA protein contains three domains: an N-terminal domain (residues 1-72) that includes a sequence of 20 hydrophobic amino acids required for membrane translocation. | + | The 326-residue Rv0899 ArfA protein from '''''Mycobacterium tuberculosis''''' [http://he.wikipedia.org/wiki/Mycobacterium_tuberculosis] contains three domains: an N-terminal domain (residues 1-72) that includes a sequence of 20 hydrophobic amino acids required for membrane translocation. |
[[Image:N-ter domain.jpg|150px]] | [[Image:N-ter domain.jpg|150px]] | ||
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= Function == | = Function == | ||
| - | The membrane protein Rv0899 ArfA | + | 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. |
<ref>PMID: 22108166 </ref> | <ref>PMID: 22108166 </ref> | ||
''Mycobacterium tuberculosis'' ArfA (Rv0899) is a membrane protein encoded by an ammonia release facilator operon that is necessary for rapid ammonia secretion, pH neutralization and adaptation to acidic environments in vitro. Its C-terminal domain (C domain) shares significant sequence homology with the OmpA-like family of peptidoglycan-binding domains, suggesting that its physiological function in acid stress protection may be related to its interaction with the mycobacterial cell wall. It exhibits pH-dependent conformational dynamics (with significant heterogeneity at neutral pH and a more ordered structure at acidic pH), which could be related to its acid stress response. The C domain associates tightly with polymeric peptidoglycan isolated from ''Mycobacterium tuberculosis''. Its functions in acid stress protection and <scene name='61/612805/The_peptidoglycan_binding_site/1'>peptidoglycan binding</scene> suggest a link between the acid stress response and the physicochemical properties of the mycobacterial cell wall.<ref>PMID: 22206986 </ref>. | ''Mycobacterium tuberculosis'' ArfA (Rv0899) is a membrane protein encoded by an ammonia release facilator operon that is necessary for rapid ammonia secretion, pH neutralization and adaptation to acidic environments in vitro. Its C-terminal domain (C domain) shares significant sequence homology with the OmpA-like family of peptidoglycan-binding domains, suggesting that its physiological function in acid stress protection may be related to its interaction with the mycobacterial cell wall. It exhibits pH-dependent conformational dynamics (with significant heterogeneity at neutral pH and a more ordered structure at acidic pH), which could be related to its acid stress response. The C domain associates tightly with polymeric peptidoglycan isolated from ''Mycobacterium tuberculosis''. Its functions in acid stress protection and <scene name='61/612805/The_peptidoglycan_binding_site/1'>peptidoglycan binding</scene> suggest a link between the acid stress response and the physicochemical properties of the mycobacterial cell wall.<ref>PMID: 22206986 </ref>. | ||
Revision as of 18:17, 15 January 2015
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