Mycobacterium tuberculosis ArfA Rv0899: Difference between revisions

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Liliya Karasik, Michal Harel, Jaime Prilusky

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	The central B domain (<scene name='61/612805/B_domain/1'>residues 73-200</scene>) <scene name='61/612805/Sheet_and_helix/1'> folds </scene> with three parallel/antiparallel alpha-helices packed against six parallel/antiparallel beta-strands that form a flat beta-sheet. 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].		The central B domain (<scene name='61/612805/B_domain/1'>residues 73-200</scene>) <scene name='61/612805/Sheet_and_helix/1'> folds </scene> with three parallel/antiparallel alpha-helices packed against six parallel/antiparallel beta-strands that form a flat beta-sheet. 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].
	<scene name='61/612805/Surface/1'>The core </scene> is hydrophobic, while the exterior is polar and predominantly acidic. The two subdomains are symmetric about α2, and their backbone atoms can be aligned with a RMSD [http://http://en.wikipedia.org/wiki/Root-mean-square_deviation] of 1.8Å, by performing a 180° rotation of either one around an axis normal to the 6-stranded β-sheet.		<scene name='61/612805/Surface/1'>The core </scene> is hydrophobic {{Template:ColorKey_Hydrophobic}}, , while the exterior is polar {{Template:ColorKey_Polar}} and predominantly acidic. The two subdomains are symmetric about α2, and their backbone atoms can be aligned with a RMSD [http://http://en.wikipedia.org/wiki/Root-mean-square_deviation] of 1.8Å, by performing a 180° rotation of either one around an axis normal to the 6-stranded β-sheet.