1pyv: Difference between revisions

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==NMR solution structure of the mitochondrial F1b presequence peptide from Nicotiana plumbaginifolia==
==NMR solution structure of the mitochondrial F1b presequence peptide from Nicotiana plumbaginifolia==
<StructureSection load='1pyv' size='340' side='right'caption='[[1pyv]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''>
<StructureSection load='1pyv' size='340' side='right'caption='[[1pyv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1pyv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leadwort-leaved_tobacco Leadwort-leaved tobacco]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PYV FirstGlance]. <br>
<table><tr><td colspan='2'>[[1pyv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_plumbaginifolia Nicotiana plumbaginifolia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PYV FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATPB OR ATP2-1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4092 Leadwort-leaved tobacco])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pyv OCA], [https://pdbe.org/1pyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pyv RCSB], [https://www.ebi.ac.uk/pdbsum/1pyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pyv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pyv OCA], [https://pdbe.org/1pyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pyv RCSB], [https://www.ebi.ac.uk/pdbsum/1pyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pyv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ATPBM_NICPL ATPBM_NICPL]] Mitochondrial membrane ATP synthase (F(1)F(0) 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. Subunits alpha and beta form the catalytic core in F(1). 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.  
[https://www.uniprot.org/uniprot/ATPBM_NICPL ATPBM_NICPL] Mitochondrial membrane ATP synthase (F(1)F(0) 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. Subunits alpha and beta form the catalytic core in F(1). 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.
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Leadwort-leaved tobacco]]
[[Category: Nicotiana plumbaginifolia]]
[[Category: Eriksson, A C]]
[[Category: Eriksson AC]]
[[Category: Glaser, E]]
[[Category: Glaser E]]
[[Category: Maler, L]]
[[Category: Maler L]]
[[Category: Moberg, P]]
[[Category: Moberg P]]
[[Category: Nilsson, S]]
[[Category: Nilsson S]]
[[Category: Stahl, A]]
[[Category: Stahl A]]
[[Category: Hydrolase]]

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