View source for 6rn5


==PptA from Streptomyces chartreusis==
<StructureSection load='6rn5' size='340' side='right'caption='[[6rn5]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rn5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_chartreusis"_(leach_et_al._1953)_preobrazhenskaya_1966 "actinomyces chartreusis" (leach et al. 1953) preobrazhenskaya 1966]. 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://proteopedia.org/fgij/fg.htm?mol=6RN5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCNRRL3882_4295 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1969 "Actinomyces chartreusis" (Leach et al. 1953) Preobrazhenskaya 1966])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rn5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Hinrichs, W]]
[[Category: Rustmeier, N H]]
[[Category: Werten, S]]
[[Category: Polyphosphate-binding protein]]
[[Category: Unknown function]]