|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2gsz' size='340' side='right'caption='[[2gsz]], [[Resolution|resolution]] 4.20Å' scene=''> | | <StructureSection load='2gsz' size='340' side='right'caption='[[2gsz]], [[Resolution|resolution]] 4.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2gsz]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GSZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2gsz]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GSZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2eyu|2eyu]], [[2ewv|2ewv]], [[2eww|2eww]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pilT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</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=2gsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gsz OCA], [https://pdbe.org/2gsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gsz RCSB], [https://www.ebi.ac.uk/pdbsum/2gsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gsz 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=2gsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gsz OCA], [https://pdbe.org/2gsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gsz RCSB], [https://www.ebi.ac.uk/pdbsum/2gsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gsz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O66950_AQUAE O66950_AQUAE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 33: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquifex aeolicus huber and stetter 2001]] | + | [[Category: Aquifex aeolicus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Forest, K T]] | + | [[Category: Forest KT]] |
| - | [[Category: Satyshur, K A]] | + | [[Category: Satyshur KA]] |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Domain motion]]
| + | |
| - | [[Category: P-loop]]
| + | |
| - | [[Category: Pa]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Reca]]
| + | |
| Structural highlights
Function
O66950_AQUAE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
PilT is a hexameric ATPase required for bacterial type IV pilus retraction and surface motility. Crystal structures of ADP- and ATP-bound Aquifex aeolicus PilT at 2.8 and 3.2 A resolution show N-terminal PAS-like and C-terminal RecA-like ATPase domains followed by a set of short C-terminal helices. The hexamer is formed by extensive polar subunit interactions between the ATPase core of one monomer and the N-terminal domain of the next. An additional structure captures a nonsymmetric PilT hexamer in which approach of invariant arginines from two subunits to the bound nucleotide forms an enzymatically competent active site. A panel of pilT mutations highlights the importance of the arginines, the PAS-like domain, the polar subunit interface, and the C-terminal helices for retraction. We present a model for ATP binding leading to dramatic PilT domain motions, engagement of the arginine wire, and subunit communication in this hexameric motor. Our conclusions apply to the entire type II/IV secretion ATPase family.
Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility.,Satyshur KA, Worzalla GA, Meyer LS, Heiniger EK, Aukema KG, Misic AM, Forest KT Structure. 2007 Mar;15(3):363-76. PMID:17355871[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Satyshur KA, Worzalla GA, Meyer LS, Heiniger EK, Aukema KG, Misic AM, Forest KT. Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Structure. 2007 Mar;15(3):363-76. PMID:17355871 doi:10.1016/j.str.2007.01.018
|
