6qv5: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6qv5 is ON HOLD  until Paper Publication
+==Crystal structure of the CHAD domain from the plant Ricinus communis==
+<StructureSection load='6qv5' size='340' side='right'caption='[[6qv5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6qv5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QV5 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCOM_0386350 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3988 Castor bean])</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=6qv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qv5 OCA], [http://pdbe.org/6qv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qv5 RCSB], [http://www.ebi.ac.uk/pdbsum/6qv5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qv5 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Inorganic polyphosphates (polyPs) are linear polymers of orthophosphate units linked by phosphoanhydride bonds. Here, we report that bacterial, archaeal, and eukaryotic conserved histidine alpha-helical (CHAD) domains are specific polyP-binding modules. Crystal structures reveal that CHAD domains are formed by two four-helix bundles, giving rise to a central pore surrounded by conserved basic surface patches. Different CHAD domains bind polyPs with dissociation constants ranging from the nano- to mid-micromolar range, but not nucleic acids. A CHAD-polyP complex structure reveals the phosphate polymer binding across the central pore and along the two basic patches. Mutational analysis of CHAD-polyP interface residues validates the complex structure. The presence of a CHAD domain in the polyPase ygiF enhances its enzymatic activity. The only known CHAD protein from the plant Ricinus communis localizes to the nucleus/nucleolus when expressed in Arabidopsis and tobacco, suggesting that plants may harbor polyPs in these compartments. We propose that CHAD domains may be used to engineer the properties of polyP-metabolizing enzymes and to specifically localize polyP stores in eukaryotic cells and tissues.
-Authors: Lorenzo-Orts, L., Hothorn, M.
+Molecular characterization of CHAD domains as inorganic polyphosphate-binding modules.,Lorenzo-Orts L, Hohmann U, Zhu J, Hothorn M Life Sci Alliance. 2019 May 27;2(3). pii: 2/3/e201900385. doi:, 10.26508/lsa.201900385. Print 2019 Jun. PMID:31133615<ref>PMID:31133615</ref>
-Description: Crystal structure of the CHAD domain from the plant Ricinus communis
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6qv5" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Castor bean]]
+[[Category: Large Structures]]
+[[Category: Hothorn, M]]
 [[Category: Lorenzo-Orts, L]]
-[[Category: Hothorn, M]]
+[[Category: All alpha-helical protein]]
+[[Category: Four-helix bundle]]
+[[Category: Inorganic polyphosphate binding protein]]
+[[Category: Nuclear protein]]