2bh5: Difference between revisions

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[[Image:2bh5.gif|left|200px]]<br /><applet load="2bh5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2bh5, resolution 1.95&Aring;" />
'''X-RAY STRUCTURE OF THE M100K VARIANT OF FERRIC CYT C-550 FROM PARACOCCUS VERSUTUS DETERMINED AT 295 K.'''<br />


==Overview==
==X-ray structure of the M100K variant of ferric cyt c-550 from Paracoccus versutus determined at 295 K.==
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.
<StructureSection load='2bh5' size='340' side='right'caption='[[2bh5]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bh5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_versutus Paracoccus versutus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BH5 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]] 1.95&#8491;</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></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=2bh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh5 OCA], [https://pdbe.org/2bh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bh5 RCSB], [https://www.ebi.ac.uk/pdbsum/2bh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bh5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CY550_PARVE CY550_PARVE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/2bh5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=2bh5 ConSurf].
<div style="clear:both"></div>
<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.


==About this Structure==
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>
2BH5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_versutus Paracoccus versutus] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Hec Binding Site For Chain X'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BH5 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15885094 15885094]
</div>
<div class="pdbe-citations 2bh5" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paracoccus versutus]]
[[Category: Paracoccus versutus]]
[[Category: Single protein]]
[[Category: Canters GW]]
[[Category: Canters, G.W.]]
[[Category: Ubbink M]]
[[Category: Roon, A.M.M.Van.]]
[[Category: Worrall JAR]]
[[Category: Ubbink, M.]]
[[Category: Van Roon A-MM]]
[[Category: Worrall, J.A.R.]]
[[Category: HEC]]
[[Category: axial ligand]]
[[Category: c-type cytochrome]]
[[Category: electron transfer]]
[[Category: heme]]
[[Category: pyrrolidone carboxylic acid]]
 
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