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| - | ==CRYSTAL STRUCTURE OF NBLA FROM PCC 7120== | + | |
| - | <StructureSection load='1ojh' size='340' side='right' caption='[[1ojh]], [[Resolution|resolution]] 1.80Å' scene=''> | + | ==Crystal structure of NblA from PCC 7120== |
| | + | <StructureSection load='1ojh' size='340' side='right'caption='[[1ojh]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ojh]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OJH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ojh]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OJH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1ojh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ojh OCA], [http://pdbe.org/1ojh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ojh RCSB], [http://www.ebi.ac.uk/pdbsum/1ojh PDBsum]</span></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=1ojh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ojh OCA], [https://pdbe.org/1ojh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ojh RCSB], [https://www.ebi.ac.uk/pdbsum/1ojh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ojh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8YNP7_NOSS1 Q8YNP7_NOSS1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena 7120]] | + | [[Category: Large Structures]] |
| - | [[Category: Baier, K]] | + | [[Category: Nostoc sp. PCC 7120 = FACHB-418]] |
| - | [[Category: Bienert, R]] | + | [[Category: Baier K]] |
| - | [[Category: Heinemann, U]] | + | [[Category: Bienert R]] |
| - | [[Category: Lockau, W]] | + | [[Category: Heinemann U]] |
| - | [[Category: Degradation protein]]
| + | [[Category: Lockau W]] |
| - | [[Category: Phycobilisome degradation]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
Q8YNP7_NOSS1
Publication Abstract from PubMed
Cyanobacterial light-harvesting complexes, the phycobilisomes, are proteolytically degraded when the organisms are starved for combined nitrogen, a process referred to as chlorosis or bleaching. Gene nblA, present in all phycobilisome-containing organisms, encodes a protein of about 7 kDa that plays a key role in phycobilisome degradation. The mode of action of NblA in this degradation process is poorly understood. Here we presented the 1.8-A crystal structure of NblA from Anabaena sp. PCC 7120. In the crystal, NblA is present as a four-helix bundle formed by dimers, the basic structural units. By using pull-down assays with immobilized NblA and peptide scanning, we showed that NblA specifically binds to the alpha-subunits of phycocyanin and phycoerythrocyanin, the main building blocks of the phycobilisome rod structure. By site-directed mutagenesis, we identified amino acid residues in NblA that are involved in phycobilisome binding. The results provided evidence that NblA is directly involved in phycobilisome degradation, and the results allowed us to present a model that gives insight into the interaction of this small protein with the phycobilisomes.
Crystal structure of NblA from Anabaena sp. PCC 7120, a small protein playing a key role in phycobilisome degradation.,Bienert R, Baier K, Volkmer R, Lockau W, Heinemann U J Biol Chem. 2006 Feb 24;281(8):5216-23. Epub 2005 Dec 15. PMID:16356935[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bienert R, Baier K, Volkmer R, Lockau W, Heinemann U. Crystal structure of NblA from Anabaena sp. PCC 7120, a small protein playing a key role in phycobilisome degradation. J Biol Chem. 2006 Feb 24;281(8):5216-23. Epub 2005 Dec 15. PMID:16356935 doi:10.1074/jbc.M507243200
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