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| | <StructureSection load='4ypn' size='340' side='right'caption='[[4ypn]], [[Resolution|resolution]] 2.07Å' scene=''> | | <StructureSection load='4ypn' size='340' side='right'caption='[[4ypn]], [[Resolution|resolution]] 2.07Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ypn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-399 Atcc baa-399]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YPN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ypn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meiothermus_taiwanensis Meiothermus taiwanensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YPN FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ypl|4ypl]], [[4ypm|4ypm]]</td></tr> | + | </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=4ypn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ypn OCA], [https://pdbe.org/4ypn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ypn RCSB], [https://www.ebi.ac.uk/pdbsum/4ypn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ypn ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lonA1, lon ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=172827 ATCC BAA-399])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ypn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ypn OCA], [http://pdbe.org/4ypn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ypn RCSB], [http://www.ebi.ac.uk/pdbsum/4ypn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ypn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A059VAZ3_9DEIN A0A059VAZ3_9DEIN]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.[HAMAP-Rule:MF_01973] | + | [https://www.uniprot.org/uniprot/A0A059VAZ3_9DEIN A0A059VAZ3_9DEIN] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.[HAMAP-Rule:MF_01973] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc baa-399]] | |
| - | [[Category: Endopeptidase La]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chang, C I]] | + | [[Category: Meiothermus taiwanensis]] |
| - | [[Category: Lin, C C]] | + | [[Category: Chang C-I]] |
| - | [[Category: Aaa+ domain]] | + | [[Category: Lin C-C]] |
| - | [[Category: Disordered]]
| + | |
| - | [[Category: Helix-bundle]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A0A059VAZ3_9DEIN ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.[HAMAP-Rule:MF_01973]
Publication Abstract from PubMed
The Lon AAA+ protease (LonA) is an evolutionarily conserved protease that couples the ATPase cycle into motion to drive substrate translocation and degradation. A hallmark feature shared by AAA+ proteases is the stimulation of ATPase activity by substrates. Here we report the structure of LonA bound to three ADPs, revealing the first AAA+ protease assembly where the six protomers are arranged alternately in nucleotide-free and bound states. Nucleotide binding induces large coordinated movements of conserved pore loops from two pairs of three non-adjacent protomers and shuttling of the proteolytic groove between the ATPase site and a previously unknown Arg paddle. Structural and biochemical evidence supports the roles of the substrate-bound proteolytic groove in allosteric stimulation of ATPase activity and the conserved Arg paddle in driving substrate degradation. Altogether, this work provides a molecular framework for understanding how ATP-dependent chemomechanical movements drive allosteric processes for substrate degradation in a major protein-destruction machine.
Structural Insights into the Allosteric Operation of the Lon AAA+ Protease.,Lin CC, Su SC, Su MY, Liang PH, Feng CC, Wu SH, Chang CI Structure. 2016 May 3;24(5):667-75. doi: 10.1016/j.str.2016.03.001. Epub 2016 Mar, 31. PMID:27041592[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lin CC, Su SC, Su MY, Liang PH, Feng CC, Wu SH, Chang CI. Structural Insights into the Allosteric Operation of the Lon AAA+ Protease. Structure. 2016 May 3;24(5):667-75. doi: 10.1016/j.str.2016.03.001. Epub 2016 Mar, 31. PMID:27041592 doi:http://dx.doi.org/10.1016/j.str.2016.03.001
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