5nlc: Difference between revisions

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-'''Unreleased structure'''
-The entry 5nlc is ON HOLD  until Paper Publication
+==Structure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942,without PLP==
+<StructureSection load='5nlc' size='340' side='right' caption='[[5nlc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5nlc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NLC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NLC FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5nlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nlc OCA], [http://pdbe.org/5nlc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nlc RCSB], [http://www.ebi.ac.uk/pdbsum/5nlc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nlc ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The Synechococcus elongatus COG0325 gene pipY functionally interacts with the nitrogen regulatory gene pipX. As a first step toward a molecular understanding of such interactions, we characterized PipY. This 221-residue protein is monomeric and hosts pyridoxal phosphate (PLP), binding it with limited affinity and losing it upon incubation with D-cycloserine. PipY crystal structures with and without PLP reveal a single-domain monomer folded as the TIM barrel of type-III fold PLP enzymes, with PLP highly exposed, fitting a role for PipY in PLP homeostasis. The mobile PLP phosphate-anchoring C-terminal helix might act as a trigger for PLP exchange. Exploiting the universality of COG0325 functions, we used PipY in site-directed mutagenesis studies to shed light on disease causation by epilepsy-associated mutations in the human COG0325 gene PROSC.
-Authors: Tremino, L., Forcada-Nadal, A., Labella, J.I., Cantos, R., Espinosa, J., Contreras, A., Rubio, V.
+Studies on cyanobacterial protein PipY shed light on structure, potential functions, and vitamin B6 -dependent epilepsy.,Tremino L, Forcada-Nadal A, Contreras A, Rubio V FEBS Lett. 2017 Sep 15. doi: 10.1002/1873-3468.12841. PMID:28914444<ref>PMID:28914444</ref>
-Description: Structure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942,without PLP
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Espinosa, J]]
+<div class="pdbe-citations 5nlc" style="background-color:#fffaf0;"></div>
-[[Category: Labella, J.I]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Contreras, A]]
+[[Category: Forcada-Nadal, A]]
 [[Category: Rubio, V]]
-[[Category: Forcada-Nadal, A]]
 [[Category: Tremino, L]]
-[[Category: Cantos, R]]
+[[Category: Fold type iii plp-protein]]
-[[Category: Contreras, A]]
+[[Category: Modified tim barrel]]
+[[Category: Plp-binding protein]]
+[[Category: Pyridoxal phosphate]]
+[[Category: Vitamin b6]]