4ii7: Difference between revisions
New page: '''Unreleased structure''' The entry 4ii7 is ON HOLD Authors: Reindl, S., Williams, G.J., Tainer, J.A. Description: Archaellum Assembly ATPase FlaI |
No edit summary |
||
| (6 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Archaellum Assembly ATPase FlaI== | |||
<StructureSection load='4ii7' size='340' side='right'caption='[[4ii7]], [[Resolution|resolution]] 3.59Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ii7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius_DSM_639 Sulfolobus acidocaldarius DSM 639]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4II7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4II7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.59Å</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=4ii7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ii7 OCA], [https://pdbe.org/4ii7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ii7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ii7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ii7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4J9L0_SULAC Q4J9L0_SULAC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Superfamily ATPases in type IV pili, type 2 secretion, and archaella (formerly archaeal flagella) employ similar sequences for distinct biological processes. Here, we structurally and functionally characterize prototypical superfamily ATPase FlaI in Sulfolobus acidocaldarius, showing FlaI activities in archaeal swimming-organelle assembly and movement. X-ray scattering data of FlaI in solution and crystal structures with and without nucleotide reveal a hexameric crown assembly with key cross-subunit interactions. Rigid building blocks form between N-terminal domains (points) and neighboring subunit C-terminal domains (crown ring). Upon nucleotide binding, these six cross-subunit blocks move with respect to each other and distinctly from secretion and pilus ATPases. Crown interactions and conformations regulate assembly, motility, and force direction via a basic-clamp switching mechanism driving conformational changes between stable, backbone-interconnected moving blocks. Collective structural and mutational results identify in vivo functional components for assembly and motility, phosphate-triggered rearrangements by ATP hydrolysis, and molecular predictors for distinct ATPase superfamily functions. | |||
Insights into FlaI Functions in Archaeal Motor Assembly and Motility from Structures, Conformations, and Genetics.,Reindl S, Ghosh A, Williams GJ, Lassak K, Neiner T, Henche AL, Albers SV, Tainer JA Mol Cell. 2013 Feb 12. pii: S1097-2765(13)00047-6. doi:, 10.1016/j.molcel.2013.01.014. PMID:23416110<ref>PMID:23416110</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ii7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sulfolobus acidocaldarius DSM 639]] | |||
[[Category: Reindl S]] | |||
[[Category: Tainer JA]] | |||
[[Category: Williams GJ]] | |||
Latest revision as of 18:23, 20 September 2023
Archaellum Assembly ATPase FlaIArchaellum Assembly ATPase FlaI
Structural highlights
FunctionPublication Abstract from PubMedSuperfamily ATPases in type IV pili, type 2 secretion, and archaella (formerly archaeal flagella) employ similar sequences for distinct biological processes. Here, we structurally and functionally characterize prototypical superfamily ATPase FlaI in Sulfolobus acidocaldarius, showing FlaI activities in archaeal swimming-organelle assembly and movement. X-ray scattering data of FlaI in solution and crystal structures with and without nucleotide reveal a hexameric crown assembly with key cross-subunit interactions. Rigid building blocks form between N-terminal domains (points) and neighboring subunit C-terminal domains (crown ring). Upon nucleotide binding, these six cross-subunit blocks move with respect to each other and distinctly from secretion and pilus ATPases. Crown interactions and conformations regulate assembly, motility, and force direction via a basic-clamp switching mechanism driving conformational changes between stable, backbone-interconnected moving blocks. Collective structural and mutational results identify in vivo functional components for assembly and motility, phosphate-triggered rearrangements by ATP hydrolysis, and molecular predictors for distinct ATPase superfamily functions. Insights into FlaI Functions in Archaeal Motor Assembly and Motility from Structures, Conformations, and Genetics.,Reindl S, Ghosh A, Williams GJ, Lassak K, Neiner T, Henche AL, Albers SV, Tainer JA Mol Cell. 2013 Feb 12. pii: S1097-2765(13)00047-6. doi:, 10.1016/j.molcel.2013.01.014. PMID:23416110[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||