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000142572 0247_ $$2pmid$$apmid:23104121
000142572 0247_ $$2doi$$a10.1007/s10863-012-9486-4
000142572 0247_ $$2ISSN$$a1573-6881
000142572 0247_ $$2ISSN$$a0145-479X
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000142572 037__ $$aPHPPUBDB-25512
000142572 041__ $$aEnglish
000142572 082__ $$a570
000142572 1001_ $$aPriya, R.$$b0
000142572 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000142572 245__ $$aSolution structure of subunit ($\gamma$ ($\gamma$1-204)) of the Mycobacterium tuberculosis F-ATP synthase and the unique loop of ($\gamma$165-178), representing a novel TB drug target
000142572 260__ $$aDordrecht [u.a.]$$bSpringer Science + Business Media B.V$$c2013
000142572 300__ $$a1-9
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000142572 3367_ $$2BibTeX$$aARTICLE
000142572 3367_ $$2ORCID$$aJOURNAL_ARTICLE
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000142572 440_0 $$0PERI:(DE-600)1482010-9$$aJournal of Bioenergetics and Biomembranes$$v45$$x0145-479X
000142572 500__ $$3Converted on 2013-05-30 09:57$$a© Springer Science+Business Media New York; Post referee fulltext in progress; Embargo 12 months from publication 
000142572 500__ $$3Converted on 2013-06-21 19:21
000142572 520__ $$aTuberculosis, caused by the strain Mycobacterium tuberculosis, is in focus of interest due to the emergence of multi- and extensive drug-resistant TB strains. The F(1)F(O) ATP synthase is one of the essential enzymes in energy requirement of both proliferating aerobic and hypoxic dormant stage of mycobacterium life cycle, and therefore a potential TB drug target. Subunit γ of F-ATP synthases plays an important role in coupling and catalysis via conformational transitions of its N- and C-termini as well as the bottom segment of the globular domain of γ, which is in close proximity to the rotating and ion-pumping c-ring. Here we describe the first production, purification and low resolution solution structure of subunit γ (γ(1-204), Mtγ(1-204)) of the M. tuberculosis F-ATP synthase. Mtγ(1-204) is a pear-like shaped protein with a molecular weight of 23 ± 2 kDa. Protein sequence analysis of Mtγ revealed differences in the amino acid composition to γ subunits from other sources, in particular the presence of a unique stretch of 13 amino acid residues (Mtγ(165-178)). NMR studies showed that Mtγ(165-178) forms a loop of polar residues. Mtγ(165-178) has been aligned at the bottom of the globular domain of the Escherichia coli subunit γ, being in close vicinity to the polar residues R41, Q42, E44 and Q46 (M. tuberculosis nomenclature) of the c-ring. The putative role(s) of Mtγ(165-178) in coupling and as a potential drug target are discussed.
000142572 536__ $$0G:(DE-H253)POF2-D1.2-20130405$$aDORIS Beamline D1.2 (POF2-54G13)$$cPOF2-54G13$$fPOF II$$x0
000142572 588__ $$aDataset connected to Pubmed
000142572 650_7 $$00$$2NLM Chemicals$$aAntitubercular Agents
000142572 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000142572 650_7 $$00$$2NLM Chemicals$$aEnzyme Inhibitors
000142572 650_7 $$00$$2NLM Chemicals$$aProtein Subunits
000142572 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000142572 650_7 $$0EC 3.6.3.14$$2NLM Chemicals$$aProton-Translocating ATPases
000142572 650_2 $$2MeSH$$aAntitubercular Agents: chemistry
000142572 650_2 $$2MeSH$$aAntitubercular Agents: therapeutic use
000142572 650_2 $$2MeSH$$aBacterial Proteins: antagonists & inhibitors
000142572 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000142572 650_2 $$2MeSH$$aBacterial Proteins: genetics
000142572 650_2 $$2MeSH$$aBacterial Proteins: metabolism
000142572 650_2 $$2MeSH$$aCatalysis
000142572 650_2 $$2MeSH$$aDrug Delivery Systems
000142572 650_2 $$2MeSH$$aEnzyme Inhibitors: chemistry
000142572 650_2 $$2MeSH$$aEnzyme Inhibitors: therapeutic use
000142572 650_2 $$2MeSH$$aMycobacterium tuberculosis: enzymology
000142572 650_2 $$2MeSH$$aMycobacterium tuberculosis: genetics
000142572 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000142572 650_2 $$2MeSH$$aProtein Structure, Secondary
000142572 650_2 $$2MeSH$$aProtein Subunits: antagonists & inhibitors
000142572 650_2 $$2MeSH$$aProtein Subunits: chemistry
000142572 650_2 $$2MeSH$$aProtein Subunits: diagnostic use
000142572 650_2 $$2MeSH$$aProtein Subunits: metabolism
000142572 650_2 $$2MeSH$$aProton-Translocating ATPases: antagonists & inhibitors
000142572 650_2 $$2MeSH$$aProton-Translocating ATPases: chemistry
000142572 650_2 $$2MeSH$$aProton-Translocating ATPases: genetics
000142572 650_2 $$2MeSH$$aProton-Translocating ATPases: metabolism
000142572 650_2 $$2MeSH$$aRecombinant Proteins: antagonists & inhibitors
000142572 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000142572 650_2 $$2MeSH$$aRecombinant Proteins: genetics
000142572 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000142572 650_2 $$2MeSH$$aTuberculosis: drug therapy
000142572 650_2 $$2MeSH$$aTuberculosis: enzymology
000142572 693__ $$0EXP:(DE-H253)D-D1.2-20150101$$1EXP:(DE-H253)DORISIII-20150101$$6EXP:(DE-H253)D-D1.2-20150101$$aDORIS III$$fDORIS Beamline D1.2$$x0
000142572 7001_ $$aBiukovic, G.$$b1
000142572 7001_ $$aManimekalai, M.$$b2
000142572 7001_ $$aLim, J.$$b3
000142572 7001_ $$aRao, S. S.$$b4
000142572 7001_ $$0P:(DE-HGF)0$$aGrueber, G.$$b5$$eCorresponding author
000142572 773__ $$0PERI:(DE-600)1482010-9$$a10.1007/s10863-012-9486-4$$gVol. 45, p. 1-9$$p1-9$$q45<1-9$$tJournal of bioenergetics and biomembranes$$v45$$x0145-479X$$y2013
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000142572 9141_ $$anot yet published$$y2013
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