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4git

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==Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber==
==Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber==
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<StructureSection load='4git' size='340' side='right' caption='[[4git]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
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<StructureSection load='4git' size='340' side='right'caption='[[4git]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4git]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_thermoruber"_guicciardi_et_al._1968 "bacillus thermoruber" guicciardi et al. 1968]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GIT FirstGlance]. <br>
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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><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lon ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33942 "Bacillus thermoruber" Guicciardi et al. 1968])</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><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>
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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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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [http://www.ebi.ac.uk/pdbsum/4git PDBsum]</span></td></tr>
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</table>
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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]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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>
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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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4git" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus thermoruber guicciardi et al. 1968]]
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[[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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