5nm8: Difference between revisions

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'''Unreleased structure'''


The entry 5nm8 is ON HOLD  until Paper Publication
==Structure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942, with PLP bound==
<StructureSection load='5nm8' size='340' side='right' caption='[[5nm8]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nm8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NM8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NM8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nlc|5nlc]]</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=5nm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nm8 OCA], [http://pdbe.org/5nm8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nm8 RCSB], [http://www.ebi.ac.uk/pdbsum/5nm8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nm8 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, with PLP bound
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 5nm8" style="background-color:#fffaf0;"></div>
[[Category: Labella, J.I]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Contreras, A]]
[[Category: Forcada-Nadal, A]]
[[Category: Rubio, V]]
[[Category: Rubio, V]]
[[Category: Forcada-Nadal, A]]
[[Category: Tremino, L]]
[[Category: Tremino, L]]
[[Category: Cantos, R]]
[[Category: Fold type iii plp-protein]]
[[Category: Contreras, A]]
[[Category: Plp-binding protein]]
[[Category: Pyridoxal phosphate]]
[[Category: Schiff base]]
[[Category: Vitamin b6]]
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