Mycobacterium tuberculosis ArfA Rv0899: Difference between revisions

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Liliya Karasik, Michal Harel, Jaime Prilusky

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	Residues <scene name='61/612805/N-c_rainbow/1'>73-326</scene> form a mixed alpha/beta-globular structure, encompassing two independently folded modules corresponding to the B and C domains connected by a flexible linker.		Residues <scene name='61/612805/N-c_rainbow/1'>73-326</scene> form a mixed alpha/beta-globular structure, encompassing two independently folded modules corresponding to the B and C domains connected by a flexible linker.

	The central B domain (<scene name='61/612805/Secondary_structure_b/1'>residues 73-200</scene>> folds ~~</scene>~~ with three parallel/antiparallel ~~alpha-~~{{Template:ColorKey_helixes}} packed against six parallel/antiparallel ~~beta-~~{{Template:ColorKey_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/Surface2/1'>The core</scene> is {{Template:ColorKey_Hydrophobic}}, while the exterior is {{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.		The central B domain (<scene name='61/612805/Secondary_structure_b/1'>residues 73-200</scene>> folds with three parallel/antiparallel {{Template:ColorKey_helixes}} packed against six parallel/antiparallel {{Template:ColorKey_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/Surface2/1'>The core</scene> is {{Template:ColorKey_Hydrophobic}}, while the exterior is {{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.