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000207433 1001_ $$0P:(DE-H253)PIP1018497$$aMa, Qingjun$$b0
000207433 245__ $$aActive Site Conformational Changes upon Reaction Intermediate Biotinyl-5'-AMP Binding in Biotin Protein Ligase from Mycobacterium Tuberculosis
000207433 260__ $$aHoboken, NJ$$bWiley$$c2014
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000207433 520__ $$aProtein biotinylation, a rare form of post-translational modification, is found in enzymes required for lipid biosynthesis. In mycobacteria, this process is essential for the formation of their complex and distinct cell wall and has become a focal point of drug discovery approaches. The enzyme responsible for this process, biotin protein ligase, substantially varies in different species in terms of overall structural organization, regulation of function and substrate specificity. To advance the understanding of the molecular mechanism of biotinylation in Mycobacterium tuberculosis we have biochemically and structurally characterized the corresponding enzyme. We report the high-resolution crystal structures of the apo-form and reaction intermediate biotinyl-5'-AMP-bound form of M. tuberculosis biotin protein ligase. Binding of the reaction intermediate leads to clear disorder-to-order transitions. We show that a conserved lysine, Lys138, in the active site is essential for biotinylation.
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000207433 536__ $$0G:(EU-Grant)241587$$aSYSTEMTB - Systems biology of Mycobacterium tuberculosis (241587)$$c241587$$fFP7-HEALTH-2009-two-stage$$x1
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000207433 7001_ $$0P:(DE-H253)PIP1013560$$aAkhter, Yusuf$$b1
000207433 7001_ $$0P:(DE-H253)PIP1001283$$aWilmanns, Matthias$$b2
000207433 7001_ $$0P:(DE-H253)PIP1014515$$aEhebauer, Matthias$$b3$$eCorresponding author
000207433 773__ $$0PERI:(DE-600)2000025-X$$a10.1002/pro.2475$$gVol. 23, no. 7, p. 932 - 939$$n7$$p932 - 939$$tProtein science$$v23$$x0961-8368$$y2014
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