5knb: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/NTPG_ENTHA NTPG_ENTHA]] Involved in ATP-driven sodium extrusion. [[http://www.uniprot.org/uniprot/NTPA_ENTHA NTPA_ENTHA]] Involved in ATP-driven sodium extrusion. [[http://www.uniprot.org/uniprot/NTPD_ENTHA NTPD_ENTHA]] Involved in ATP-driven sodium extrusion.<ref>PMID:8157629</ref> [[http://www.uniprot.org/uniprot/NTPB_ENTHA NTPB_ENTHA]] Involved in ATP-driven sodium extrusion. | [[http://www.uniprot.org/uniprot/NTPG_ENTHA NTPG_ENTHA]] Involved in ATP-driven sodium extrusion. [[http://www.uniprot.org/uniprot/NTPA_ENTHA NTPA_ENTHA]] Involved in ATP-driven sodium extrusion. [[http://www.uniprot.org/uniprot/NTPD_ENTHA NTPD_ENTHA]] Involved in ATP-driven sodium extrusion.<ref>PMID:8157629</ref> [[http://www.uniprot.org/uniprot/NTPB_ENTHA NTPB_ENTHA]] Involved in ATP-driven sodium extrusion. | ||
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== Publication Abstract from PubMed == | |||
V1-ATPases are highly conserved ATP-driven rotary molecular motors found in various membrane systems. We recently reported the crystal structures for the Enterococcus hirae A3B3DF (V1) complex, corresponding to the catalytic dwell state waiting for ATP hydrolysis. Here we present the crystal structures for two other dwell states obtained by soaking nucleotide-free V1 crystals in ADP. In the presence of 20 muM ADP, two ADP molecules bind to two of three binding sites and cooperatively induce conformational changes of the third site to an ATP-binding mode, corresponding to the ATP-binding dwell. In the presence of 2 mM ADP, all nucleotide-binding sites are occupied by ADP to induce conformational changes corresponding to the ADP-release dwell. Based on these and previous findings, we propose a V1-ATPase rotational mechanism model. | |||
Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor.,Suzuki K, Mizutani K, Maruyama S, Shimono K, Imai FL, Muneyuki E, Kakinuma Y, Ishizuka-Katsura Y, Shirouzu M, Yokoyama S, Yamato I, Murata T Nat Commun. 2016 Oct 27;7:13235. doi: 10.1038/ncomms13235. PMID:27807367<ref>PMID:27807367</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:38, 10 December 2016
Crystal structure of the 2 ADP-bound V1 complexCrystal structure of the 2 ADP-bound V1 complex
Structural highlights
Function[NTPG_ENTHA] Involved in ATP-driven sodium extrusion. [NTPA_ENTHA] Involved in ATP-driven sodium extrusion. [NTPD_ENTHA] Involved in ATP-driven sodium extrusion.[1] [NTPB_ENTHA] Involved in ATP-driven sodium extrusion. Publication Abstract from PubMedV1-ATPases are highly conserved ATP-driven rotary molecular motors found in various membrane systems. We recently reported the crystal structures for the Enterococcus hirae A3B3DF (V1) complex, corresponding to the catalytic dwell state waiting for ATP hydrolysis. Here we present the crystal structures for two other dwell states obtained by soaking nucleotide-free V1 crystals in ADP. In the presence of 20 muM ADP, two ADP molecules bind to two of three binding sites and cooperatively induce conformational changes of the third site to an ATP-binding mode, corresponding to the ATP-binding dwell. In the presence of 2 mM ADP, all nucleotide-binding sites are occupied by ADP to induce conformational changes corresponding to the ADP-release dwell. Based on these and previous findings, we propose a V1-ATPase rotational mechanism model. Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor.,Suzuki K, Mizutani K, Maruyama S, Shimono K, Imai FL, Muneyuki E, Kakinuma Y, Ishizuka-Katsura Y, Shirouzu M, Yokoyama S, Yamato I, Murata T Nat Commun. 2016 Oct 27;7:13235. doi: 10.1038/ncomms13235. PMID:27807367[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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