2xt4: Difference between revisions
Jump to navigation
Jump to search
m Protected "2xt4" [edit=sysop:move=sysop] |
No edit summary |
||
| (6 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==Structure of the pentapeptide repeat protein AlbG, a resistance factor for the topoisomerase poison albicidin.== | ||
<StructureSection load='2xt4' size='340' side='right'caption='[[2xt4]], [[Resolution|resolution]] 2.39Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xt4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_albilineans Xanthomonas albilineans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XT4 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]] 2.394Å</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=2xt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xt4 OCA], [https://pdbe.org/2xt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xt4 RCSB], [https://www.ebi.ac.uk/pdbsum/2xt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xt4 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q70C34_XANAL Q70C34_XANAL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The protein AlbG is a self-resistance factor against albicidin, a nonribosomally encoded hybrid polyketide-peptide with antibiotic and phytotoxic properties produced by Xanthomonas albilineans. Primary-sequence analysis indicates that AlbG is a member of the pentapeptide-repeat family of proteins (PRP). The structure of AlbG from X. albilineans was determined at 2.0 A resolution by SAD phasing using data collected from a single trimethyllead acetate derivative on a home source. AlbG folds into a right-handed quadrilateral beta-helix composed of approximately eight semi-regular coils. The regularity of the beta-helix is blemished by a large loop/deviation in the beta-helix between coils 4 and 5. The C-terminus of the beta-helix is capped by a dimerization module, yielding a dimer with a 110 A semi-collinear beta-helical axis. This method of dimer formation appears to be common to all PRP proteins that confer resistance to topoisomerase poisons and contrasts with most PRP proteins, which are typically monomeric. | |||
Pentapeptide-repeat proteins that act as topoisomerase poison resistance factors have a common dimer interface.,Vetting MW, Hegde SS, Zhang Y, Blanchard JS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt, 3):296-302. Epub 2011 Feb 18. PMID:21393830<ref>PMID:21393830</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xt4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Xanthomonas albilineans]] | [[Category: Xanthomonas albilineans]] | ||
[[Category: Blanchard | [[Category: Blanchard JS]] | ||
[[Category: Hegde | [[Category: Hegde SS]] | ||
[[Category: Vetting | [[Category: Vetting MW]] | ||
Latest revision as of 11:03, 23 August 2023
Structure of the pentapeptide repeat protein AlbG, a resistance factor for the topoisomerase poison albicidin.Structure of the pentapeptide repeat protein AlbG, a resistance factor for the topoisomerase poison albicidin.
Structural highlights
FunctionPublication Abstract from PubMedThe protein AlbG is a self-resistance factor against albicidin, a nonribosomally encoded hybrid polyketide-peptide with antibiotic and phytotoxic properties produced by Xanthomonas albilineans. Primary-sequence analysis indicates that AlbG is a member of the pentapeptide-repeat family of proteins (PRP). The structure of AlbG from X. albilineans was determined at 2.0 A resolution by SAD phasing using data collected from a single trimethyllead acetate derivative on a home source. AlbG folds into a right-handed quadrilateral beta-helix composed of approximately eight semi-regular coils. The regularity of the beta-helix is blemished by a large loop/deviation in the beta-helix between coils 4 and 5. The C-terminus of the beta-helix is capped by a dimerization module, yielding a dimer with a 110 A semi-collinear beta-helical axis. This method of dimer formation appears to be common to all PRP proteins that confer resistance to topoisomerase poisons and contrasts with most PRP proteins, which are typically monomeric. Pentapeptide-repeat proteins that act as topoisomerase poison resistance factors have a common dimer interface.,Vetting MW, Hegde SS, Zhang Y, Blanchard JS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt, 3):296-302. Epub 2011 Feb 18. PMID:21393830[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||