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[[Image:3cs5.png|left|200px]]


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==NblA protein from Synechococcus elongatus PCC 7942==
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<StructureSection load='3cs5' size='340' side='right'caption='[[3cs5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3cs5]] is a 4 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=3CS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CS5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cs5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cs5 OCA], [https://pdbe.org/3cs5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cs5 RCSB], [https://www.ebi.ac.uk/pdbsum/3cs5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cs5 ProSAT]</span></td></tr>
{{STRUCTURE_3cs5|  PDB=3cs5  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/NBLA_SYNE7 NBLA_SYNE7] Involved in phycobilisome (PBS) degradation during nutrient deprivation. May mark the PBS for degradation by covalent association with PBS components or may disrupt the PBS via ionic interactions.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enormous macromolecular phycobilisome antenna complex (&gt;4 MDa) in cyanobacteria and red algae undergoes controlled degradation during certain forms of nutrient starvation. The NblA protein (approximately 6 kDa) has been identified as an essential component in this process. We have used structural, biochemical, and genetic methods to obtain molecular details on the mode of action of the NblA protein. We have determined the three-dimensional structure of the NblA protein from both the thermophilic cyanobacterium Thermosynechococcus vulcanus and the mesophilic cyanobacterium Synechococcus elongatus sp. PCC 7942. The NblA monomer has a helix-loop-helix motif which dimerizes into an open, four-helical bundle, identical to the previously determined NblA structure from Anabaena. Previous studies indicated that mutations to NblA residues near the C terminus impaired its binding to phycobilisome proteins in vitro, whereas the only mutation known to affect NblA function in vivo is located near the protein N terminus. We performed random mutagenesis of the S. elongatus nblA gene which enabled the identification of four additional amino acids crucial for NblA function in vivo. This data shows that essential amino acids are not confined to the protein termini. We also show that expression of the Anabaena nblA gene complements phycobilisome degradation in an S. elongatus NblA-null mutant despite the low homology between NblAs of these cyanobacteria. We propose that the NblA interacts with the phycobilisome via "structural mimicry" due to similarity in structural motifs found in all phycobiliproteins. This suggestion leads to a new model for the mode of NblA action which involves the entire NblA protein.


===NblA protein from Synechococcus elongatus PCC 7942===
Structural, functional, and mutational analysis of the NblA protein provides insight into possible modes of interaction with the phycobilisome.,Dines M, Sendersky E, David L, Schwarz R, Adir N J Biol Chem. 2008 Oct 31;283(44):30330-40. Epub 2008 Aug 21. PMID:18718907<ref>PMID:18718907</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
{{ABSTRACT_PUBMED_18718907}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3CS5 is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CS5 OCA].
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
 
[[Category: Adir N]]
==Reference==
[[Category: Dines M]]
<ref group="xtra">PMID:18718907</ref><ref group="xtra">PMID:17187990</ref><references group="xtra"/>
[[Category: Schwarz R]]
[[Category: Synechococcus sp.]]
[[Category: Sendersky E]]
[[Category: Adir, N.]]
[[Category: Dines, M.]]
[[Category: Schwarz, R.]]
[[Category: Sendersky, E.]]
[[Category: Bleaching]]
[[Category: Helix-turn-helix]]
[[Category: Nutrient stress]]
[[Category: Partial merohedral twinning]]
[[Category: Photosynthesis]]
[[Category: Phycobilisome]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 17 09:43:53 2010''

Latest revision as of 17:59, 1 November 2023

NblA protein from Synechococcus elongatus PCC 7942NblA protein from Synechococcus elongatus PCC 7942

Structural highlights

3cs5 is a 4 chain structure with sequence from Synechococcus elongatus PCC 7942 = FACHB-805. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NBLA_SYNE7 Involved in phycobilisome (PBS) degradation during nutrient deprivation. May mark the PBS for degradation by covalent association with PBS components or may disrupt the PBS via ionic interactions.

Publication Abstract from PubMed

The enormous macromolecular phycobilisome antenna complex (>4 MDa) in cyanobacteria and red algae undergoes controlled degradation during certain forms of nutrient starvation. The NblA protein (approximately 6 kDa) has been identified as an essential component in this process. We have used structural, biochemical, and genetic methods to obtain molecular details on the mode of action of the NblA protein. We have determined the three-dimensional structure of the NblA protein from both the thermophilic cyanobacterium Thermosynechococcus vulcanus and the mesophilic cyanobacterium Synechococcus elongatus sp. PCC 7942. The NblA monomer has a helix-loop-helix motif which dimerizes into an open, four-helical bundle, identical to the previously determined NblA structure from Anabaena. Previous studies indicated that mutations to NblA residues near the C terminus impaired its binding to phycobilisome proteins in vitro, whereas the only mutation known to affect NblA function in vivo is located near the protein N terminus. We performed random mutagenesis of the S. elongatus nblA gene which enabled the identification of four additional amino acids crucial for NblA function in vivo. This data shows that essential amino acids are not confined to the protein termini. We also show that expression of the Anabaena nblA gene complements phycobilisome degradation in an S. elongatus NblA-null mutant despite the low homology between NblAs of these cyanobacteria. We propose that the NblA interacts with the phycobilisome via "structural mimicry" due to similarity in structural motifs found in all phycobiliproteins. This suggestion leads to a new model for the mode of NblA action which involves the entire NblA protein.

Structural, functional, and mutational analysis of the NblA protein provides insight into possible modes of interaction with the phycobilisome.,Dines M, Sendersky E, David L, Schwarz R, Adir N J Biol Chem. 2008 Oct 31;283(44):30330-40. Epub 2008 Aug 21. PMID:18718907[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Dines M, Sendersky E, David L, Schwarz R, Adir N. Structural, functional, and mutational analysis of the NblA protein provides insight into possible modes of interaction with the phycobilisome. J Biol Chem. 2008 Oct 31;283(44):30330-40. Epub 2008 Aug 21. PMID:18718907 doi:10.1074/jbc.M804241200

3cs5, resolution 2.20Å

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