Mycobacterium tuberculosis ArfA Rv0899
From Proteopedia
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Protein Rv0899 from '''''Mycobacterium tuberculosis''''' [http://he.wikipedia.org/wiki/Mycobacterium_tuberculosis] belongs to the OmpA (outer membrane protein A) family of outer membrane proteins.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 Zn(2+) ions, which may indicate a role for Rv0899 in the process of Zn(2+) acquisition. | Protein Rv0899 from '''''Mycobacterium tuberculosis''''' [http://he.wikipedia.org/wiki/Mycobacterium_tuberculosis] belongs to the OmpA (outer membrane protein A) family of outer membrane proteins.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 Zn(2+) ions, 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'' 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 peptidoglycan binding suggest a link between the acid stress response and the physicochemical properties of the mycobacterial cell wall.<ref>PMID: 22206986 </ref>. |
== Disease == | == Disease == | ||
Rv0899 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 gene is restricted to pathogenic mycobacteria and, thus, is an attractive candidate for the development of anti-tuberculosis chemotherapy. <ref>PMID: 20199110</ref> | Rv0899 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 gene is restricted to pathogenic mycobacteria and, thus, is an attractive candidate for the development of anti-tuberculosis chemotherapy. <ref>PMID: 20199110</ref> | ||
| - | Probably plays a role in ammonia secretion that neutralizes the medium at pH 5.5,and preceded exponential growth of | + | Probably plays a role in ammonia secretion that neutralizes the medium at pH 5.5,and preceded exponential growth of ''Mycobacterium tuberculosis'', although it does not play a direct role in ammonia transport.[[http://www.uniprot.org/uniprot/P9WIU5 ARFA_MYCTU]]. The ompATb operon is necessary for rapid ammonia secretion and adaptation of M. tuberculosis to acidic environments in vitro but not in mice. |
<ref>PMID: 21410778 </ref> | <ref>PMID: 21410778 </ref> | ||
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<scene name='61/612805/Asn111_and_gly112/1'>Deamidation between Asn111 and Gly112 causing to ammonia releasing</scene> | <scene name='61/612805/Asn111_and_gly112/1'>Deamidation between Asn111 and Gly112 causing to ammonia releasing</scene> | ||
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<scene name='61/612805/The_peptidoglycan_binding_site/1'>The peptidoglycan binding site</scene> | <scene name='61/612805/The_peptidoglycan_binding_site/1'>The peptidoglycan binding site</scene> | ||
Revision as of 13:42, 4 January 2015
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