4eic

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<StructureSection load='4eic' size='340' side='right'caption='[[4eic]], [[Resolution|resolution]] 0.84&Aring;' scene=''>
<StructureSection load='4eic' size='340' side='right'caption='[[4eic]], [[Resolution|resolution]] 0.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4eic]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agmenellum_quadruplicatum Agmenellum quadruplicatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EIC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4eic]] 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=4EIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EIC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dr0|3dr0]], [[4eid|4eid]], [[4eie|4eie]], [[4eif|4eif]]</div></td></tr>
 
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">petJ, petJ1, SYNPCC7002_A0167 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32049 Agmenellum quadruplicatum])</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=4eic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eic OCA], [https://pdbe.org/4eic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eic RCSB], [https://www.ebi.ac.uk/pdbsum/4eic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eic ProSAT]</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=4eic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eic OCA], [https://pdbe.org/4eic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eic RCSB], [https://www.ebi.ac.uk/pdbsum/4eic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eic ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CYC6_SYNP2 CYC6_SYNP2]] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis (By similarity).
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[https://www.uniprot.org/uniprot/CYC6_SYNP2 CYC6_SYNP2] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the reduced form of cytochrome c(6) from the mesophilic cyanobacterium Synechococcus sp. PCC 7002 has been determined at 1.2 A and refined to an R-factor of 0.107. This protein is unique among all known cytochromes c(6), owing to the presence of an unusual seven-residue insertion, KDGSKSL(44-50), which differs from the insertion found in the recently discovered plant cytochromes c(6A). Furthermore, the present protein is unusual because of its very high content (36%) of the smallest residues (glycine and alanine). The structure reveals that the overall fold of the protein is similar to that of other class I c-type cytochromes, despite the presence of the specific insertion. The insertion is located within the most variable region of the cytochrome c(6) sequence, i.e. between helices II and III. The first six residues [KDGSKS(44-49)] form a loop, whereas the last residue, Leu50, extends the N-terminal beginning of helix III. Several specific noncovalent interactions are found inside the insertion, as well as between the insertion and the rest of the protein. The crystal structure contains three copies of the cytochrome c(6) molecule per asymmetric unit, and is characterized by an unusually high packing density, with solvent occupying barely 17.58% of the crystal volume.
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Atomic-resolution structure of reduced cyanobacterial cytochrome c6 with an unusual sequence insertion.,Bialek W, Krzywda S, Jaskolski M, Szczepaniak A FEBS J. 2009 Aug;276(16):4426-36. PMID:19678839<ref>PMID:19678839</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4eic" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 
*[[Cytochrome f 3D structures|Cytochrome f 3D structures]]
*[[Cytochrome f 3D structures|Cytochrome f 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Agmenellum quadruplicatum]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bialek, W]]
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[[Category: Synechococcus sp. PCC 7002]]
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[[Category: Jaskolski, M]]
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[[Category: Bialek W]]
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[[Category: Krzywda, S]]
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[[Category: Jaskolski M]]
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[[Category: Szczepaniak, A]]
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[[Category: Krzywda S]]
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[[Category: Cytochrome c6]]
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[[Category: Szczepaniak A]]
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[[Category: Electron transport]]
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Revision as of 10:40, 14 December 2022

Crystal structure of reduced cytochrome c6 from Synechococcus sp. PCC 7002 at ultra-high resolution

PDB ID 4eic

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