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4git

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{{STRUCTURE_4git| PDB=4git | SCENE= }}
 
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===Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber===
 
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==Function==
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==Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber==
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[[http://www.uniprot.org/uniprot/Q84FG5_9BACL Q84FG5_9BACL]] 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 (By similarity).[HAMAP-Rule:MF_01973]
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<StructureSection load='4git' size='340' side='right'caption='[[4git]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4git]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_thermoruber Brevibacillus thermoruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GIT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.882&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [https://pdbe.org/4git PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [https://www.ebi.ac.uk/pdbsum/4git PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4git ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q84FG5_9BACL Q84FG5_9BACL] 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 (By similarity).[HAMAP-Rule:MF_01973]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Lon belongs to a unique group of AAA+ proteases that bind DNA. However, the DNA-mediated regulation of Lon remains elusive. Here, the crystal structure of the alpha subdomain of the Lon protease from Brevibacillus thermoruber (Bt-Lon) is presented, together with biochemical data, and the DNA-binding mode is delineated, showing that Arg518, Arg557 and Arg566 play a crucial role in DNA binding. Electrostatic interactions contributed by arginine residues in the AAA+ module are suggested to be important to DNA binding and allosteric regulation of enzymatic activities. Intriguingly, Arg557, which directly binds DNA in the alpha subdomain, has a dual role in the negative regulation of ATPase stimulation by DNA and in the domain-domain communication in allosteric regulation of Bt-Lon by substrate. In conclusion, structural and biochemical evidence is provided to show that electrostatic interaction in the AAA+ module is important for DNA binding by Lon and allosteric regulation of its enzymatic activities by DNA and substrate.
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==About this Structure==
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Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease.,Lee AY, Chen YD, Chang YY, Lin YC, Chang CF, Huang SJ, Wu SH, Hsu CH Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):218-30. doi:, 10.1107/S139900471302631X. Epub 2014 Jan 17. PMID:24531457<ref>PMID:24531457</ref>
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[[4git]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brevibacillus_thermoruber Brevibacillus thermoruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA].
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4git" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Brevibacillus thermoruber]]
[[Category: Brevibacillus thermoruber]]
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[[Category: Endopeptidase La]]
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[[Category: Large Structures]]
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[[Category: Chang, Y Y.]]
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[[Category: Chang YY]]
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[[Category: Chen, Y D.]]
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[[Category: Chen YD]]
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[[Category: Hsu, C H.]]
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[[Category: Hsu CH]]
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[[Category: Dna binding]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber

PDB ID 4git

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