4git: Difference between revisions

(5 intermediate revisions by the same user not shown)

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 4git is ~~ON HOLD until Paper~~ Publication

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

== Structural highlights ==

<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>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.882Å</td></tr>

<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>

<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>

</table>

== Function ==

[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]

== Publication Abstract from PubMed ==

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.

~~Authors:~~ Chen, ~~Y.D.~~, Chang, Y.Y., ~~Hsu, C~~.H.

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>

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Brevibacillus thermoruber]]

[[Category: Large Structures]]

[[Category: Chang YY]]

[[Category: Chen YD]]

[[Category: Hsu CH]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4git is ON HOLD  until Paper Publication
+==Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber==
+<StructureSection load='4git' size='340' side='right'caption='[[4git]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== Function ==
+[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;">
+== Publication Abstract from PubMed ==
+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.
-Authors: Chen, Y.D., Chang, Y.Y., Hsu, C.H.
+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>
-Description: Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4git" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Brevibacillus thermoruber]]
+[[Category: Large Structures]]
+[[Category: Chang YY]]
+[[Category: Chen YD]]
+[[Category: Hsu CH]]