DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu How azide inhibits ATP hydrolysis by the F-ATPases. How azide inhibits ATP hydrolysis by the F-ATPases. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Bowler MW., Montgomery MG., Leslie AG., Walker JE. Only protein-protein interactions bovin Bos taurus (Bovine) Bovine x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bowler MW., Montgomery MG., Leslie AG., Walker JE. DIP original experiment: DIP-263163X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx How azide inhibits ATP hydrolysis by the F-ATPases. atpb_bovin ATP synthase subunit beta, mitochondrial ATP5F1B ATP synthase F1 subunit beta ATP5B protein protein bovin Bos taurus (Bovine) Bovine MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDYAAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS DIP protein P00829 original sequence version: 152 DIP protein P00829 original sequence version: 93 DIP protein P00829 original sequence version: 92 DIP protein P00829 original sequence version: 109 DIP protein P00829 original sequence version: 125 DIP protein P00829 original sequence version: 134 32218D14A5497F18 atp5e_bovin ATP synthase subunit epsilon, mitochondrial ATP5F1E ATP synthase F1 subunit epsilon ATP5E protein protein bovin Bos taurus (Bovine) Bovine MVAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE DIP protein P05632 original sequence version: 134 DIP protein P05632 original sequence version: 81 DIP protein P05632 original sequence version: 96 DIP protein P05632 original sequence version: 109 DIP protein P05632 original sequence version: 118 mint Mitochondrial membrane ATP synthase (F(1)F(O) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits E0D70FA7C9191CAE atpa_bovin ATP synthase subunit alpha, mitochondrial ATP5F1A ATP synthase F1 subunit alpha ATP5A1 ATP5A2 protein protein bovin Bos taurus (Bovine) Bovine MLSVRVAAAVARALPRRAGLVSKNALGSSFIAARNLHASNSRLQKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALLSKIRTDGKISEESDAKLKEIVTNFLAGFEA DIP protein P19483 original sequence version: 148 DIP protein P19483 original sequence version: 91 DIP protein P19483 original sequence version: 90 DIP protein P19483 original sequence version: 106 DIP protein P19483 original sequence version: 124 DIP protein P19483 original sequence version: 132 188E9531B3B815E0 atpd_bovin ATP synthase subunit delta, mitochondrial ATP5F1D ATP synthase F1 subunit delta ATP5D F-ATPase delta subunit protein protein bovin Bos taurus (Bovine) Bovine MLPSALLRRPGLGRLVRQVRLYAEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELLGAADEATRAEIQIRIEANEALVKALE DIP protein P05630 original sequence version: 127 DIP protein P05630 original sequence version: 79 DIP protein P05630 original sequence version: 94 DIP protein P05630 original sequence version: 107 DIP protein P05630 original sequence version: 113 7C47BBAD5A151608 atpg_bovin ATP synthase subunit gamma, mitochondrial ATP5F1C ATP synthase F1 subunit gamma ATP5C ATP5C1 F-ATPase gamma subunit protein protein bovin Bos taurus (Bovine) Bovine MFSRAGVAGLSAWTVQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTPEDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTHSDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFSLDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAALD DIP protein P05631 original sequence version: 140 DIP protein P05631 original sequence version: 105 DIP protein P05631 original sequence version: 118 DIP protein P05631 original sequence version: 124 mint Mitochondrial membrane ATP synthase (F(1)F(O) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits C1F41767CDABAD92 atp5a1-atp5b-2 1 3 unspecified role unspecified role unspecified role unspecified role Region 2-51 Region 2-51 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain bovin Bos taurus (Bovine) Bovine 6 unspecified role unspecified role unspecified role unspecified role Region 26-297 Region 26-297 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain bovin Bos taurus (Bovine) Bovine 5 unspecified role unspecified role unspecified role unspecified role Region 23-168 Region 23-168 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain bovin Bos taurus (Bovine) Bovine 2 unspecified role unspecified role unspecified role unspecified role Region 47-528 Region 47-528 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain bovin Bos taurus (Bovine) Bovine 4 unspecified role unspecified role unspecified role unspecified role Region 44-553 Region 44-553 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain bovin Bos taurus (Bovine) Bovine physical association physical association