4git

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Revision as of 06:27, 5 August 2016

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

Structural highlights

4git is a 2 chain structure with sequence from "bacillus_thermoruber"_guicciardi_et_al._1968 "bacillus thermoruber" guicciardi et al. 1968. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	lon ("Bacillus thermoruber" Guicciardi et al. 1968)
Activity:	Endopeptidase La, with EC number 3.4.21.53
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

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^[1]

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

References

↑ Lee AY, Chen YD, Chang YY, Lin YC, Chang CF, Huang SJ, Wu SH, Hsu CH. Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):218-30. doi:, 10.1107/S139900471302631X. Epub 2014 Jan 17. PMID:24531457 doi:http://dx.doi.org/10.1107/S139900471302631X

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4git"

@@ Line 1: / Line 1: @@
 ==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=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><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>
 <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=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>
+<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=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [http://pdbe.org/4git PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [http://www.ebi.ac.uk/pdbsum/4git PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4git ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 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/>

4git

From Proteopedia

Revision as of 06:27, 5 August 2016

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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