4eif: Difference between revisions
New page: '''Unreleased structure''' The entry 4eif is ON HOLD Authors: Krzywda, S., Bialek, W., Zatwarnicki, P., Jaskolski, M., Szczepaniak, A. Description: Crystal structure of cytochrome c6C ... |
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The | ==Crystal structure of cytochrome c6C L50Q mutant from Synechococcus sp. PCC 7002== | ||
<StructureSection load='4eif' size='340' side='right'caption='[[4eif]], [[Resolution|resolution]] 1.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4eif]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._PCC_7002 Synechococcus sp. PCC 7002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EIF 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]] 1.04Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4eif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eif OCA], [https://pdbe.org/4eif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eif RCSB], [https://www.ebi.ac.uk/pdbsum/4eif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eif ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8KX15_PICP2 Q8KX15_PICP2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The cyanobacterium Synechococcus sp. PCC 7002 carries two genes, petJ1 and petJ2, for proteins related to soluble, cytochrome c6 electron transfer proteins. PetJ1 was purified from the cyanobacterium, and both cytochromes were expressed with heme incorporation in Escherichia coli. The expressed PetJ1 displayed spectral and biochemical properties virtually identical to those of PetJ1 from Synechococcus. PetJ1 is a typical cytochrome c6 but contains an unusual KDGSKSL insertion. PetJ2 isolated from E. coli exhibited absorbance spectra characteristic of cytochromes, although the alpha, beta, and gamma bands were red-shifted relative to those of PetJ1. Moreover, the surface electrostatic properties and redox midpoint potential of PetJ2 (pI 9.7; E(m,7) = 148 +/- 1.7 mV) differed substantially from those of PetJ1 (pI 3.8; E(m,7) = 319 +/- 1.6 mV). These data indicate that the PetJ2 cytochrome could not effectively replace PetJ1 as an electron acceptor for the cytochrome bf complex in photosynthesis. Phylogenetic comparisons against plant, algal, bacterial, and cyanobacterial genomes revealed two novel and widely distributed clusters of previously uncharacterized, cyanobacterial c 6-like cytochromes. PetJ2 belongs to a group that is distinct from both c6 cytochromes and the enigmatic chloroplast c 6A cytochromes. We tentatively designate the PetJ2 group as c6C cytochromes and the other new group as c6B cytochromes. Possible functions of these cytochromes are discussed. | |||
Deeply branching c6-like cytochromes of cyanobacteria.,Bialek W, Nelson M, Tamiola K, Kallas T, Szczepaniak A Biochemistry. 2008 May 20;47(20):5515-22. Epub 2008 Apr 26. PMID:018439023<ref>PMID:018439023</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4eif" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechococcus sp. PCC 7002]] | |||
[[Category: Bialek W]] | |||
[[Category: Jaskolski M]] | |||
[[Category: Krzywda S]] | |||
[[Category: Szczepaniak A]] | |||
[[Category: Zatwarnicki P]] | |||
Latest revision as of 12:58, 30 October 2024
Crystal structure of cytochrome c6C L50Q mutant from Synechococcus sp. PCC 7002Crystal structure of cytochrome c6C L50Q mutant from Synechococcus sp. PCC 7002
Structural highlights
FunctionPublication Abstract from PubMedThe cyanobacterium Synechococcus sp. PCC 7002 carries two genes, petJ1 and petJ2, for proteins related to soluble, cytochrome c6 electron transfer proteins. PetJ1 was purified from the cyanobacterium, and both cytochromes were expressed with heme incorporation in Escherichia coli. The expressed PetJ1 displayed spectral and biochemical properties virtually identical to those of PetJ1 from Synechococcus. PetJ1 is a typical cytochrome c6 but contains an unusual KDGSKSL insertion. PetJ2 isolated from E. coli exhibited absorbance spectra characteristic of cytochromes, although the alpha, beta, and gamma bands were red-shifted relative to those of PetJ1. Moreover, the surface electrostatic properties and redox midpoint potential of PetJ2 (pI 9.7; E(m,7) = 148 +/- 1.7 mV) differed substantially from those of PetJ1 (pI 3.8; E(m,7) = 319 +/- 1.6 mV). These data indicate that the PetJ2 cytochrome could not effectively replace PetJ1 as an electron acceptor for the cytochrome bf complex in photosynthesis. Phylogenetic comparisons against plant, algal, bacterial, and cyanobacterial genomes revealed two novel and widely distributed clusters of previously uncharacterized, cyanobacterial c 6-like cytochromes. PetJ2 belongs to a group that is distinct from both c6 cytochromes and the enigmatic chloroplast c 6A cytochromes. We tentatively designate the PetJ2 group as c6C cytochromes and the other new group as c6B cytochromes. Possible functions of these cytochromes are discussed. Deeply branching c6-like cytochromes of cyanobacteria.,Bialek W, Nelson M, Tamiola K, Kallas T, Szczepaniak A Biochemistry. 2008 May 20;47(20):5515-22. Epub 2008 Apr 26. PMID:018439023[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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