View source for 5nlc


==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 with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5NLC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5nlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nlc OCA], [https://pdbe.org/5nlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nlc RCSB], [https://www.ebi.ac.uk/pdbsum/5nlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nlc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q31LH9_SYNE7 Q31LH9_SYNE7] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nlc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
[[Category: Contreras A]]
[[Category: Forcada-Nadal A]]
[[Category: Rubio V]]
[[Category: Tremino L]]