1qzm

From Proteopedia

(Difference between revisions)

Revision as of 06:35, 5 April 2017

alpha-domain of ATPase

Structural highlights

1qzm is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Endopeptidase La, with EC number 3.4.21.53
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LON_ECOLI] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. 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. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD. Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the small, mostly helical alpha domain of the AAA+ module of the Escherichia coli ATP-dependent protease Lon has been solved by single isomorphous replacement combined with anomalous scattering and refined at 1.9A resolution to a crystallographic R factor of 17.9%. This domain, comprising residues 491-584, was obtained by chymotrypsin digestion of the recombinant full-length protease. The alpha domain of Lon contains four alpha helices and two parallel strands and resembles similar domains found in a variety of ATPases and helicases, including the oligomeric proteases HslVU and ClpAP. The highly conserved "sensor-2" Arg residue is located at the beginning of the third helix. Detailed comparison with the structures of 11 similar domains established the putative location of the nucleotide-binding site in this first fragment of Lon for which a crystal structure has become available.

Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution.,Botos I, Melnikov EE, Cherry S, Khalatova AG, Rasulova FS, Tropea JE, Maurizi MR, Rotanova TV, Gustchina A, Wlodawer A J Struct Biol. 2004 Apr-May;146(1-2):113-22. PMID:15037242^[4]

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

References

↑ Thomas-Wohlever J, Lee I. Kinetic characterization of the peptidase activity of Escherichia coli Lon reveals the mechanistic similarities in ATP-dependent hydrolysis of peptide and protein substrates. Biochemistry. 2002 Jul 30;41(30):9418-25. PMID:12135363
↑ Vineyard D, Patterson-Ward J, Lee I. Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease. Biochemistry. 2006 Apr 11;45(14):4602-10. PMID:16584195 doi:10.1021/bi052377t
↑ Duval V, Nicoloff H, Levy SB. Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli. Antimicrob Agents Chemother. 2009 Nov;53(11):4944-8. doi: 10.1128/AAC.00787-09., Epub 2009 Aug 31. PMID:19721064 doi:10.1128/AAC.00787-09
↑ Botos I, Melnikov EE, Cherry S, Khalatova AG, Rasulova FS, Tropea JE, Maurizi MR, Rotanova TV, Gustchina A, Wlodawer A. Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution. J Struct Biol. 2004 Apr-May;146(1-2):113-22. PMID:15037242 doi:10.1016/j.jsb.2003.09.003

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qzm"

@@ Line 1: / Line 1: @@
 ==alpha-domain of ATPase==
 <StructureSection load='1qzm' size='340' side='right' caption='[[1qzm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qzm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QZM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qzm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QZM FirstGlance]. <br>
-</td></tr><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=562 "Bacillus coli" Migula 1895])</td></tr>
+</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='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=1qzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzm OCA], [http://pdbe.org/1qzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qzm RCSB], [http://www.ebi.ac.uk/pdbsum/1qzm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzm ProSAT]</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=1qzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzm OCA], [http://pdbe.org/1qzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qzm RCSB], [http://www.ebi.ac.uk/pdbsum/1qzm PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
 [[Category: Endopeptidase La]]
 [[Category: Botos, I]]

1qzm

From Proteopedia

Revision as of 06:35, 5 April 2017

alpha-domain of ATPase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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