Mycobacterium tuberculosis ArfA Rv0899
From Proteopedia
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<StructureSection load='2l26' size='350' side='right' caption='NMR structure of uncharacterized protein Rv0899 (PDB code [[2l26]])' scene='61/612805/N-c_rainbow/1'> | <StructureSection load='2l26' size='350' side='right' caption='NMR structure of uncharacterized protein Rv0899 (PDB code [[2l26]])' scene='61/612805/N-c_rainbow/1'> | ||
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==Introduction== | ==Introduction== | ||
| + | The protein Rv0899 ArfA is restricted to pathogenic Mycobacteria associated with tuberculosis and, thus, is an attractive candidate for the development of anti-tuberculosis chemotherapeutic agents.The 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]]. The deletion of this gene impairs the uptake of some water-soluble substances, such as serine, glucose, and glycerol. | ||
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==Peptidoglycan binding site== | ==Peptidoglycan binding site== | ||
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==Function== | ==Function== | ||
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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. | ||
<ref>PMID: 22108166 </ref> | <ref>PMID: 22108166 </ref> | ||
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[[Image:MurNac11.jpg|150px]] | [[Image:MurNac11.jpg|150px]] | ||
| - | + | Two M. tuberculosis H37Rv genes (Rv0900 and Rv0901) adjacent to Rv0899 also encode putative membrane proteins, and are found exclusively in association with Rv0899 in the same pathogenic mycobacteria, suggesting that the three may constitute an operon dedicated to a common function. The operon is necessary for rapid ammonia secretion and adaptation of M. tuberculosis to acidic environments in vitro but not in mice. | |
Asparagine is the primary ammonia source for Mycobacterium tuberculosis H37Rv at acidic pH <ref>PMID: 21410778 </ref>. The amino acid pair <scene name='61/612805/Asn111_and_gly112/1'>Asn111-Gly112</scene>,located at the end of α1 and preceding L3, undergoes in-vitro deamidation, a pH-dependent reaction whereby Asn is converted to Asp and ammonia is released. Asparagine residues preceding glycine, and situated in conformationally flexible regions of proteins, are frequently deamidated, with potentially significant consequences for protein regulation and function. In the case of Rv0899, deamidation and the concomitant release of ammonia could have important consequences for the acid adaptation function of the protein. <ref>PMID: 20199110</ref> | Asparagine is the primary ammonia source for Mycobacterium tuberculosis H37Rv at acidic pH <ref>PMID: 21410778 </ref>. The amino acid pair <scene name='61/612805/Asn111_and_gly112/1'>Asn111-Gly112</scene>,located at the end of α1 and preceding L3, undergoes in-vitro deamidation, a pH-dependent reaction whereby Asn is converted to Asp and ammonia is released. Asparagine residues preceding glycine, and situated in conformationally flexible regions of proteins, are frequently deamidated, with potentially significant consequences for protein regulation and function. In the case of Rv0899, deamidation and the concomitant release of ammonia could have important consequences for the acid adaptation function of the protein. <ref>PMID: 20199110</ref> | ||
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<scene name='61/612805/Positive-negativ_aa/1'>TextToBeDisplayed</scene> | <scene name='61/612805/Positive-negativ_aa/1'>TextToBeDisplayed</scene> | ||
<scene name='61/612805/C_domain_stabilization/1'>TextToBeDisplayed</scene> | <scene name='61/612805/C_domain_stabilization/1'>TextToBeDisplayed</scene> | ||
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| + | [[Image:Rv0899 memb arch.jpg|150px]] | ||
| + | [[Image:180 rotation BON.jpg|150px]] | ||
Revision as of 15:53, 21 January 2015
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