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1gxi

From Proteopedia

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Revision as of 07:13, 17 January 2018

PsaE Subunit of the Photosystem I of the Cyanobacterium Synechocystis sp. PCC 6803

Structural highlights

1gxi is a 1 chain structure with sequence from Synechocystis sp.. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PSAE_SYNY3] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.[HAMAP-Rule:MF_00613]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

PsaE is a small peripheral subunit of photosystem I (PSI) that is very accessible to the surrounding medium. It plays an essential role in optimizing the interactions with the soluble electron acceptors of PSI, ferredoxin and flavodoxin. The solution structure of PsaE from the cyanobacterium Synechocystis sp. PCC 6803 has been investigated by NMR with a special emphasis on its protein dynamic properties. PsaE is characterized by a well-defined central core that consists of a five-stranded beta-sheet (+1, +1, +1, -4x). Four loops (designated the A-B, B-C, C-D, and D-E loops) connect these beta-strands, the overall resulting structure being that of an SH3-like domain. As compared to previously determined PsaE structures, conformational differences are observed in the first three loops. The flexibility of the loops was investigated using (15)N relaxation experiments. This flexibility is small in amplitude for the A-B and B-C loops, but is large for the C-D loop, particularly in the region corresponding to the missing sequence of Nostoc sp. PCC 8009. The plasticity of the connecting loops in the free subunit is compared to that when bound to the PSI and discussed in relation to the insertion process and the function(s) of PsaE.

Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I from Synechocystis sp. PCC 6803.,Barth P, Savarin P, Gilquin B, Lagoutte B, Ochsenbein F Biochemistry. 2002 Nov 26;41(47):13902-14. PMID:12437347^[1]

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

References

↑ Barth P, Savarin P, Gilquin B, Lagoutte B, Ochsenbein F. Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I from Synechocystis sp. PCC 6803. Biochemistry. 2002 Nov 26;41(47):13902-14. PMID:12437347

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gxi"

@@ Line 1: / Line 1: @@
-==PsaE sub-unit of the photosystem I of the cyanobacterium Synechocystis sp. PCC 6803==
+==PsaE Subunit of the Photosystem I of the Cyanobacterium Synechocystis sp. PCC 6803==
 <StructureSection load='1gxi' size='340' side='right' caption='[[1gxi]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''>
 == Structural highlights ==
@@ Line 12: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/1gxi_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/1gxi_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 27: / Line 27: @@
 </div>
 <div class="pdbe-citations 1gxi" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Photosystem I|Photosystem I]]
 == References ==
 <references/>

1gxi

From Proteopedia

Revision as of 07:13, 17 January 2018

PsaE Subunit of the Photosystem I of the Cyanobacterium Synechocystis sp. PCC 6803

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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