|
|
| Line 1: |
Line 1: |
| | | | |
| | ==CRYSTAL STRUCTURE OF THE 14-3-3:NEUTRAL TREHALASE NTH1 COMPLEX== | | ==CRYSTAL STRUCTURE OF THE 14-3-3:NEUTRAL TREHALASE NTH1 COMPLEX== |
| - | <StructureSection load='5n6n' size='340' side='right' caption='[[5n6n]], [[Resolution|resolution]] 2.29Å' scene=''> | + | <StructureSection load='5n6n' size='340' side='right'caption='[[5n6n]], [[Resolution|resolution]] 2.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5n6n]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N6N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5n6n]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N6N 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=SUC:SUCROSE'>SUC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMH1, YER177W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), NTH1, NTH, YDR001C, YD8119.07C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=5n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n6n OCA], [https://pdbe.org/5n6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n6n RCSB], [https://www.ebi.ac.uk/pdbsum/5n6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n6n ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha,alpha-trehalase Alpha,alpha-trehalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.28 3.2.1.28] </span></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=5n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n6n OCA], [http://pdbe.org/5n6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n6n RCSB], [http://www.ebi.ac.uk/pdbsum/5n6n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n6n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BMH1_YEAST BMH1_YEAST]] Involved in growth regulation. | + | [https://www.uniprot.org/uniprot/BMH1_YEAST BMH1_YEAST] Involved in growth regulation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha,alpha-trehalase]] | + | [[Category: Large Structures]] |
| - | [[Category: Baker's yeast]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Alblova, M]] | + | [[Category: Alblova M]] |
| - | [[Category: Obsil, T]] | + | [[Category: Obsil T]] |
| - | [[Category: Obsilova, V]] | + | [[Category: Obsilova V]] |
| - | [[Category: Smidova, A]] | + | [[Category: Smidova A]] |
| - | [[Category: 14-3-3]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Neutral trehalase]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
5n6n is a 3 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.29Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
BMH1_YEAST Involved in growth regulation.
Publication Abstract from PubMed
The 14-3-3 proteins, a family of highly conserved scaffolding proteins ubiquitously expressed in all eukaryotic cells, interact with and regulate the function of several hundreds of partner proteins. Yeast neutral trehalases (Nth), enzymes responsible for the hydrolysis of trehalose to glucose, compared with trehalases from other organisms, possess distinct structure and regulation involving phosphorylation at multiple sites followed by binding to the 14-3-3 protein. Here we report the crystal structures of yeast Nth1 and its complex with Bmh1 (yeast 14-3-3 isoform), which, together with mutational and fluorescence studies, indicate that the binding of Nth1 by 14-3-3 triggers Nth1's activity by enabling the proper 3D configuration of Nth1's catalytic and calcium-binding domains relative to each other, thus stabilizing the flexible part of the active site required for catalysis. The presented structure of the Bmh1:Nth1 complex highlights the ability of 14-3-3 to modulate the structure of a multidomain binding partner and to function as an allosteric effector. Furthermore, comparison of the Bmh1:Nth1 complex structure with those of 14-3-3:serotonin N-acetyltransferase and 14-3-3:heat shock protein beta-6 complexes revealed similarities in the 3D structures of bound partner proteins, suggesting the highly conserved nature of 14-3-3 affects the structures of many client proteins.
Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.,Alblova M, Smidova A, Docekal V, Vesely J, Herman P, Obsilova V, Obsil T Proc Natl Acad Sci U S A. 2017 Oct 30. pii: 201714491. doi:, 10.1073/pnas.1714491114. PMID:29087344[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alblova M, Smidova A, Docekal V, Vesely J, Herman P, Obsilova V, Obsil T. Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1. Proc Natl Acad Sci U S A. 2017 Oct 30. pii: 201714491. doi:, 10.1073/pnas.1714491114. PMID:29087344 doi:http://dx.doi.org/10.1073/pnas.1714491114
|
