Mycobacterium tuberculosis ArfA Rv0899: Difference between revisions

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Liliya Karasik, Michal Harel, Jaime Prilusky

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-. binding to peptidoglycan and phospholipid layer.
+. Binding to peptidoglycan and phospholipid layer.
-a) The B domain has homology with conserved putative <scene name='61/612805/Conserved_g95_and_g164_in_bon/2'>lipid-binding BON</scene> (bacterial OsmY and nodulation) superfamily domains and conserved Gly95 and Gly164 [http://www.ebi.ac.uk/interpro/entry/IPR014004], which putative function is phospolipid binding, nitrogen fixation and / or nitrogen metabolism <ref>PMID: 12878000 </ref>.
+a) The B domain has homology with conserved putative <scene name='61/612805/Conserved_g95_and_g164_in_bon/2'>lipid-binding BON</scene> (bacterial OsmY and nodulation) superfamily domains and conserved Gly95 and Gly164 [http://www.ebi.ac.uk/interpro/entry/IPR014004], which putative functions are prevention of shrinkage of inner and outer membrane by binding to the phospholipid layer, nitrogen fixation and / or nitrogen metabolism <ref>PMID: 12878000 </ref>.
-b)The C domain has homology to the OmpA-C-like superfamily of periplasmic peptidoglycan-binding sequences, found in several types of bacterial membrane proteins.Contribution for structural strength to the bacterial cell wall under acid or other stress conditionsIts functions by binding to peptidoglycan biosyntheesis intermediate uridine-5-'-diphosphate-MurNAc–L-Ala–D-γ-Glu–m-DAP–D-Ala–D-Ala (UMDP) [http://en.wikipedia.org/wiki/Peptidoglycan] binding site. <scene name='61/612805/Peptidoglycan_binding_site/1'>(R277, R319, T261, D262, N270)</scene>. These residues are strictly conserved in the OmpA -like family The side chain of m-DAP is stabilized by charge-charge interactions between its electronegative carbonyl group with R277 and R319 guanidinium groups and with the N270 carboxamide and between its electropositive amino group with the D262 carboxyl and the T261 hydroxyl. UMDP could interact through contacts of its γ-Glu3 and Ala2 backbone amides with the side-chain hydroxyl of S266, of its MurNAc O3 with the amide proton of E267, and of its MurNAc NH2 with the E267 carboxyl <ref>PMID: 22206986 </ref>.
+b)The C domain has homology to the OmpA-C-like superfamily of periplasmic peptidoglycan-binding sequences, found in several types of bacterial membrane proteins.Contribution for structural strength to the bacterial cell wall under acid or other stress conditionsIts functions by binding to peptidoglycan biosyntheesis intermediate uridine-5-'-diphosphate-MurNAc–L-Ala–D-γ-Glu–m-DAP–D-Ala–D-Ala (UMDP) [http://en.wikipedia.org/wiki/Peptidoglycan] binding site. <scene name='61/612805/Peptidoglycan_binding_site/1'>(R277, R319, T261, D262, N270)</scene>. These residues are strictly conserved in the OmpA -like family. The side chain of m-DAP is stabilized by charge-charge interactions between its electronegative carbonyl group with R277 and R319 guanidinium groups and with the N270 carboxamide and between its electropositive amino group with the D262 carboxyl and the T261 hydroxyl. UMDP could interact through contacts of its γ-Glu3 and Ala2 backbone amides with the side-chain hydroxyl of S266, of its MurNAc O3 with the amide proton of E267, and of its MurNAc NH2 with the E267 carboxyl <ref>PMID: 22206986 </ref>.
 [[Image:123456.jpg|250px]]                              [[Image:MurNac11.jpg|250px]]