2bgv

==X-RAY STRUCTURE OF FERRIC CYTOCHROME C-550 FROM PARACOCCUS VERSUTUS==

<StructureSection load='2bgv' size='340' side='right' caption='[[2bgv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[2bgv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25364 Atcc 25364]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BGV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BGV FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bh4|2bh4]], [[2bh5|2bh5]]</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=2bgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bgv OCA], [http://pdbe.org/2bgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bgv RCSB], [http://www.ebi.ac.uk/pdbsum/2bgv PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/2bgv_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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

== Publication Abstract from PubMed ==

The structure of cytochrome c-550 from the nonphotosynthetic bacteria Paraccocus versutus has been solved by X-ray crystallography to 1.90 A resolution, and reveals a high structural homology to other bacterial cytochromes c(2). The effect of replacing the axial heme-iron methionine ligand with a lysine residue on protein structure and unfolding has been assessed using the M100K variant. From X-ray structures at 1.95 and 1.55 A resolution it became clear that the amino group of the lysine side chain coordinates to the heme-iron. Structural differences compared to the wild-type protein are confined to the lysine ligand loop connecting helices four and five. In the heme cavity an additional water molecule is found which participates in an H-bonding interaction with the lysine ligand. Under cryo-conditions extra electron density in the lysine ligand loop is revealed, leading to residues K97 to T101 being modeled with a double main-chain conformation. Upon unfolding, dissociation of the lysine ligand from the heme-iron is shown to be pH dependent, with NMR data consistent with the occurrence of a ligand exchange mechanism similar to that seen for the wild-type protein.

The effect of replacing the axial methionine ligand with a lysine residue in cytochrome c-550 from Paracoccus versutus assessed by X-ray crystallography and unfolding.,Worrall JA, van Roon AM, Ubbink M, Canters GW FEBS J. 2005 May;272(10):2441-55. PMID:15885094<ref>PMID:15885094</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2bgv" style="background-color:#fffaf0;"></div>

*[[Cytochrome c|Cytochrome c]]

[[Category: Atcc 25364]]

[[Category: Canters, G W]]

[[Category: Roon, A M.M Van]]

[[Category: Ubbink, M]]

[[Category: Worrall, J A.R]]

[[Category: C-type cytochrome]]

[[Category: Electron transfer]]

[[Category: Pyrrolidone carboxylic acid]]