5daz: Difference between revisions
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==Crystal structure of Scabin, a mono-ADP-ribosyltransferase from Streptomyces scabies== | |||
<StructureSection load='5daz' size='340' side='right'caption='[[5daz]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5daz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_scabiei_87.22 Streptomyces scabiei 87.22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DAZ 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]] 1.45Å</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=5daz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5daz OCA], [https://pdbe.org/5daz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5daz RCSB], [https://www.ebi.ac.uk/pdbsum/5daz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5daz ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C9Z6T8_STRSW C9Z6T8_STRSW] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A bioinformatics strategy was used to identify Scabin, a novel DNA-targeting enzyme from the plant pathogen 87.22 strain of Streptomyces scabies. Scabin shares nearly 40% sequence identity with the Pierisin family of mono-ADP-ribosyltransferase toxins. Scabin was purified to homogeneity as a 22-kDa single-domain enzyme and was shown to possess high NAD+-glycohydrolase (KM(NAD) = 68 +/- 3 microM; kcat = 94 +/- 2 min-1) activity with an R-S-Q-X-E motif; it was also shown to target deoxyguanosine and showed sigmoidal enzyme kinetics (K0.5(deoxyguanosine) = 302 +/- 12 microM; kcat = 14 min-1). Mass spectrometry analysis revealed that Scabin labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA. Several small molecule inhibitors were identified and the most potent compounds were found to inhibit the enzyme activity with Ki values ranging from 3 to 24 microM. PJ34, a well-known inhibitor of poly-ADP-ribosyltransferases, was shown to be the most potent inhibitor of Scabin. Scabin was crystallized and it represents the first structure of a DNA-targeting mono-ADP-ribosyltransferase enzyme; the structures of the apo form (1.45A) and with two inhibitors (P6-E, 1.4A; PJ34, 1.6A) were solved. These structures are also the first high-resolution models of the Pierisin subgroup of the mono-ADP-ribosyltransferase toxin family. A model of Scabin with its DNA substrate is also proposed. | |||
Scabin, a novel DNA-acting ADP-ribosyltransferase from Streptomyces scabies.,Lyons B, Ravulapalli R, Lanoue J, Lugo MR, Dutta D, Carlin S, Merrill AR J Biol Chem. 2016 Mar 21. pii: jbc.M115.707653. PMID:27002155<ref>PMID:27002155</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5daz" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces scabiei 87 22]] | |||
[[Category: Dutta D]] | |||
[[Category: Lanoue J]] | |||
[[Category: Merrill AR]] | |||
Latest revision as of 11:44, 27 September 2023
Crystal structure of Scabin, a mono-ADP-ribosyltransferase from Streptomyces scabiesCrystal structure of Scabin, a mono-ADP-ribosyltransferase from Streptomyces scabies
Structural highlights
FunctionPublication Abstract from PubMedA bioinformatics strategy was used to identify Scabin, a novel DNA-targeting enzyme from the plant pathogen 87.22 strain of Streptomyces scabies. Scabin shares nearly 40% sequence identity with the Pierisin family of mono-ADP-ribosyltransferase toxins. Scabin was purified to homogeneity as a 22-kDa single-domain enzyme and was shown to possess high NAD+-glycohydrolase (KM(NAD) = 68 +/- 3 microM; kcat = 94 +/- 2 min-1) activity with an R-S-Q-X-E motif; it was also shown to target deoxyguanosine and showed sigmoidal enzyme kinetics (K0.5(deoxyguanosine) = 302 +/- 12 microM; kcat = 14 min-1). Mass spectrometry analysis revealed that Scabin labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA. Several small molecule inhibitors were identified and the most potent compounds were found to inhibit the enzyme activity with Ki values ranging from 3 to 24 microM. PJ34, a well-known inhibitor of poly-ADP-ribosyltransferases, was shown to be the most potent inhibitor of Scabin. Scabin was crystallized and it represents the first structure of a DNA-targeting mono-ADP-ribosyltransferase enzyme; the structures of the apo form (1.45A) and with two inhibitors (P6-E, 1.4A; PJ34, 1.6A) were solved. These structures are also the first high-resolution models of the Pierisin subgroup of the mono-ADP-ribosyltransferase toxin family. A model of Scabin with its DNA substrate is also proposed. Scabin, a novel DNA-acting ADP-ribosyltransferase from Streptomyces scabies.,Lyons B, Ravulapalli R, Lanoue J, Lugo MR, Dutta D, Carlin S, Merrill AR J Biol Chem. 2016 Mar 21. pii: jbc.M115.707653. PMID:27002155[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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