4eic

<StructureSection load='4eic' size='340' side='right' caption='[[4eic]], [[Resolution|resolution]] 0.84&Aring;' scene=''>

<table><tr><td colspan='2'>[[4eic]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EIC FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dr0|3dr0]], [[4eid|4eid]], [[4eie|4eie]], [[4eif|4eif]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">petJ, petJ1, SYNPCC7002_A0167 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32049 Synechococcus sp. PCC 7002])</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=4eic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eic OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eic RCSB], [http://www.ebi.ac.uk/pdbsum/4eic PDBsum]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

 

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>

 

*[[Cytochrome c|Cytochrome c]]

[[Category: Synechococcus sp. pcc 7002]]

[[Category: Bialek, W]]

[[Category: Jaskolski, M]]

[[Category: Krzywda, S]]

[[Category: Szczepaniak, A]]

[[Category: Electron transport]]