6rn5: Difference between revisions
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==PptA from Streptomyces chartreusis== | |||
<StructureSection load='6rn5' size='340' side='right'caption='[[6rn5]], [[Resolution|resolution]] 2.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rn5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RN5 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rn5 OCA], [http://pdbe.org/6rn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rn5 RCSB], [http://www.ebi.ac.uk/pdbsum/6rn5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rn5 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
X-ray crystallographic analysis of a phosin (PptA) from Steptomyces chartreusis reveals a metal-associated, lozenge-shaped fold featuring a 5-10 A wide, positively charged tunnel that traverses the protein core. Two distinct metal-binding sites were identified in which the predominant metal ion was Cu(2+) . In solution, PptA forms stable homodimers that bind with nanomolar affinity to polyphosphate, a stress-related biopolymer acting as a phosphate and energy reserve in conditions of nutrient depletion. A single protein dimer interacts with 14-15 consecutive phosphate moieties within the polymer. Our observations suggest that PptA plays a role in polyphosphate metabolism, mobilisation or sensing, possibly by acting in concert with polyphosphate kinase (Ppk). Like Ppk, phosins may influence antibiotic synthesis by streptomycetes. | |||
Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold.,Werten S, Rustmeier NH, Gemmer M, Virolle MJ, Hinrichs W FEBS Lett. 2019 Jun 10. doi: 10.1002/1873-3468.13476. PMID:31183865<ref>PMID:31183865</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6rn5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Hinrichs, W]] | |||
[[Category: Rustmeier, N]] | |||
[[Category: Werten, S]] | |||
[[Category: Polyphosphate-binding protein]] | |||
[[Category: Unknown function]] | |||
Revision as of 06:17, 19 June 2019
PptA from Streptomyces chartreusis
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