5nm8
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==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]] 1.93Å' 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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 5nm8" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Contreras, A]] | ||
[[Category: Forcada-Nadal, A]] | [[Category: Forcada-Nadal, A]] | ||
+ | [[Category: Rubio, V]] | ||
[[Category: Tremino, L]] | [[Category: Tremino, L]] | ||
- | [[Category: | + | [[Category: Fold type iii plp-protein]] |
- | [[Category: | + | [[Category: Plp-binding protein]] |
+ | [[Category: Pyridoxal phosphate]] | ||
+ | [[Category: Schiff base]] | ||
+ | [[Category: Vitamin b6]] |
Revision as of 09:16, 27 September 2017
Structure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942, with PLP bound
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