Mycobacterium tuberculosis ArfA Rv0899: Difference between revisions

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b) PH-dependent conformational dynamics of hydrophobic cluster of 232, 225, 240, 244, 281, 285 <scene name='61/612805/D236_before_mutation/1'>in neutral pH (D236) </scene> and a more ordered structure like a flap at <scene name='61/612805/D236a_after_mut/3'>acidic pH (D236A) </scene>.
b) pH-dependent conformational dynamics of hydrophobic cluster of L232, F225, L240, A244, V281, L285 <scene name='61/612805/D236_before_mutation/1'>in neutral pH (D236) </scene> and a more ordered structure like a flap at <scene name='61/612805/D236a_after_mut/3'>acidic pH (D236A) </scene>.


Its functions in acid stress protection and [peptidoglycan][http://en.wikipedia.org/wiki/Peptidoglycan] binding site <scene name='61/612805/Peptidoglycan_binding_site/1'>(R277, R319, T261, D262, N270)</scene> suggest a link between the acid stress response and the physicochemical properties of the mycobacterial cell wall. These residues are strictly conserved in the OmpA -like family <ref>PMID: 22206986 </ref>.  
Its functions in acid stress protection and [peptidoglycan][http://en.wikipedia.org/wiki/Peptidoglycan] binding site <scene name='61/612805/Peptidoglycan_binding_site/1'>(R277, R319, T261, D262, N270)</scene> suggest a link between the acid stress response and the physicochemical properties of the mycobacterial cell wall. These residues are strictly conserved in the OmpA -like family <ref>PMID: 22206986 </ref>.  

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Liliya Karasik, Michal Harel, Jaime Prilusky