001     142572
005     20250730151051.0
024 7 _ |a pmid:23104121
|2 pmid
024 7 _ |a 10.1007/s10863-012-9486-4
|2 doi
024 7 _ |a 1573-6881
|2 ISSN
024 7 _ |a 0145-479X
|2 ISSN
024 7 _ |a WOS:000314899500011
|2 WOS
024 7 _ |a openalex:W2277704780
|2 openalex
037 _ _ |a PHPPUBDB-25512
041 _ _ |a English
082 _ _ |a 570
100 1 _ |a Priya, R.
|b 0
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a Solution 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
260 _ _ |a Dordrecht [u.a.]
|c 2013
|b Springer Science + Business Media B.V
300 _ _ |a 1-9
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1524565479_1391
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
440 _ 0 |a Journal of Bioenergetics and Biomembranes
|0 PERI:(DE-600)1482010-9
|v 45
|x 0145-479X
500 _ _ |a © Springer Science+Business Media New York; Post referee fulltext in progress; Embargo 12 months from publication
|3 Converted on 2013-05-30 09:57
500 _ _ |3 Converted on 2013-06-21 19:21
520 _ _ |a Tuberculosis, 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.
536 _ _ |0 G:(DE-H253)POF2-D1.2-20130405
|f POF II
|x 0
|c POF2-54G13
|a DORIS Beamline D1.2 (POF2-54G13)
588 _ _ |a Dataset connected to Pubmed
650 _ 7 |a Antitubercular Agents
|0 0
|2 NLM Chemicals
650 _ 7 |a Bacterial Proteins
|0 0
|2 NLM Chemicals
650 _ 7 |a Enzyme Inhibitors
|0 0
|2 NLM Chemicals
650 _ 7 |a Protein Subunits
|0 0
|2 NLM Chemicals
650 _ 7 |a Recombinant Proteins
|0 0
|2 NLM Chemicals
650 _ 7 |a Proton-Translocating ATPases
|0 EC 3.6.3.14
|2 NLM Chemicals
650 _ 2 |a Antitubercular Agents: chemistry
|2 MeSH
650 _ 2 |a Antitubercular Agents: therapeutic use
|2 MeSH
650 _ 2 |a Bacterial Proteins: antagonists & inhibitors
|2 MeSH
650 _ 2 |a Bacterial Proteins: chemistry
|2 MeSH
650 _ 2 |a Bacterial Proteins: genetics
|2 MeSH
650 _ 2 |a Bacterial Proteins: metabolism
|2 MeSH
650 _ 2 |a Catalysis
|2 MeSH
650 _ 2 |a Drug Delivery Systems
|2 MeSH
650 _ 2 |a Enzyme Inhibitors: chemistry
|2 MeSH
650 _ 2 |a Enzyme Inhibitors: therapeutic use
|2 MeSH
650 _ 2 |a Mycobacterium tuberculosis: enzymology
|2 MeSH
650 _ 2 |a Mycobacterium tuberculosis: genetics
|2 MeSH
650 _ 2 |a Nuclear Magnetic Resonance, Biomolecular
|2 MeSH
650 _ 2 |a Protein Structure, Secondary
|2 MeSH
650 _ 2 |a Protein Subunits: antagonists & inhibitors
|2 MeSH
650 _ 2 |a Protein Subunits: chemistry
|2 MeSH
650 _ 2 |a Protein Subunits: diagnostic use
|2 MeSH
650 _ 2 |a Protein Subunits: metabolism
|2 MeSH
650 _ 2 |a Proton-Translocating ATPases: antagonists & inhibitors
|2 MeSH
650 _ 2 |a Proton-Translocating ATPases: chemistry
|2 MeSH
650 _ 2 |a Proton-Translocating ATPases: genetics
|2 MeSH
650 _ 2 |a Proton-Translocating ATPases: metabolism
|2 MeSH
650 _ 2 |a Recombinant Proteins: antagonists & inhibitors
|2 MeSH
650 _ 2 |a Recombinant Proteins: chemistry
|2 MeSH
650 _ 2 |a Recombinant Proteins: genetics
|2 MeSH
650 _ 2 |a Recombinant Proteins: metabolism
|2 MeSH
650 _ 2 |a Tuberculosis: drug therapy
|2 MeSH
650 _ 2 |a Tuberculosis: enzymology
|2 MeSH
693 _ _ |a DORIS III
|f DORIS Beamline D1.2
|1 EXP:(DE-H253)DORISIII-20150101
|0 EXP:(DE-H253)D-D1.2-20150101
|6 EXP:(DE-H253)D-D1.2-20150101
|x 0
700 1 _ |a Biukovic, G.
|b 1
700 1 _ |a Manimekalai, M.
|b 2
700 1 _ |a Lim, J.
|b 3
700 1 _ |a Rao, S. S.
|b 4
700 1 _ |a Grueber, G.
|0 P:(DE-HGF)0
|b 5
|e Corresponding author
773 _ _ |a 10.1007/s10863-012-9486-4
|g Vol. 45, p. 1-9
|0 PERI:(DE-600)1482010-9
|q 45<1-9
|p 1-9
|t Journal of bioenergetics and biomembranes
|v 45
|y 2013
|x 0145-479X
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909 C O |p VDB
|o oai:bib-pubdb1.desy.de:142572
913 1 _ |b Struktur der Materie
|1 G:(DE-HGF)POF2-540
|0 G:(DE-HGF)POF2-54G13
|2 G:(DE-HGF)POF2-500
|v DORIS III
|9 G:(DE-H253)POF2-D1.2-20130405
|x 0
|a DE-H253
|4 G:(DE-HGF)POF
|3 G:(DE-HGF)POF2
|l Forschung mit Photonen, Neutronen, Ionen
914 1 _ |a not yet published
|y 2013
915 _ _ |a Medline
|0 StatID:(DE-HGF)0300
|2 StatID
915 _ _ |a No Author Disambiguation
|0 StatID:(DE-HGF)1
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920 _ _ |k 001
920 1 _ |0 I:(DE-H253)EMBL_-2012_-20130307
|k EMBL(-2012)
|l EMBL
|x 0
920 _ 1 |i European Molecular Biology Laboratory
|k EMBL
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a I:(DE-H253)EMBL_-2012_-20130307
980 _ _ |a UNRESTRICTED


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