5nlc: Difference between revisions
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New page: '''Unreleased structure''' The entry 5nlc is ON HOLD until Paper Publication Authors: Tremino, L., Forcada-Nadal, A., Labella, J.I., Cantos, R., Espinosa, J., Contreras, A., Rubio, V. ... |
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==Structure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942,without PLP== | |||
<StructureSection load='5nlc' size='340' side='right'caption='[[5nlc]], [[Resolution|resolution]] 1.90Å' 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]] 1.9Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 5nlc" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Forcada-Nadal | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]] | |||
[[Category: Contreras A]] | |||
[[Category: Forcada-Nadal A]] | |||
[[Category: Rubio V]] | |||
[[Category: Tremino L]] | |||
Latest revision as of 16:05, 15 November 2023
Structure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942,without PLPStructure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942,without PLP
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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