3ph2: Difference between revisions

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[[Image:3ph2.png|left|200px]]
==Structure of the imidazole-adduct of the Phormidium laminosum cytochrome c6 Q51V variant==
<StructureSection load='3ph2' size='340' side='right' caption='[[3ph2]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ph2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phormidium_laminosum Phormidium laminosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PH2 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=IMD:IMIDAZOLE'>IMD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v08|2v08]]</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=3ph2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ph2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ph2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ph2 PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The amino acid at position 51 in the cytochrome c (6) family is responsible for modulating over 100 mV of heme midpoint redox potential. As part of the present work, the X-ray structure of the imidazole adduct of the photosynthetic cytochrome c (6) Q51V variant from Phormidium laminosum has been determined. The structure reveals the axial Met ligand is dissociated from the heme iron but remains inside the heme pocket and the Omega-loop housing the Met ligand is stabilized through polar interactions with the imidazole and heme propionate-6. The latter is possible owing to a 180 degrees rotation of both heme propionates upon imidazole binding. From equilibrium and kinetic studies, a Val residue at position 51 increases the stability of the Fe-S(Met) interaction and also affects the dynamics associated with imidazole binding. In this respect, the k (obs) for imidazole binding to Arabidopsis thaliana cytochrome c (6A), which has a Val at the position equivalent to position 51 in photosynthetic cytochrome c (6), was found to be independent of imidazole concentration, indicating that the binding process is limited by the Met dissociation rate constant (about 1 s(-1)). For the cytochrome c (6) Q51V variant, imidazole binding was suppressed in comparison with the wild-type protein and the V52Q variant of cytochrome c (6A) was found to bind imidazole readily. We conclude that the residue type at position 51/52 in the cytochrome c (6) family is additionally responsible for tuning the stability of the heme iron-Met bond and the dynamic properties of the ferric protein fold associated with endogenous ligand binding.


{{STRUCTURE_3ph2|  PDB=3ph2  |  SCENE=  }}
Structural and kinetic studies of imidazole binding to two members of the cytochrome c (6) family reveal an important role for a conserved heme pocket residue.,Rajagopal BS, Wilson MT, Bendall DS, Howe CJ, Worrall JA J Biol Inorg Chem. 2011 Jan 26. PMID:21267610<ref>PMID:21267610</ref>


===Structure of the imidazole-adduct of the Phormidium laminosum cytochrome c6 Q51V variant===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_21267610}}
 
==About this Structure==
[[3ph2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phormidium_laminosum Phormidium laminosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PH2 OCA].


==See Also==
==See Also==
*[[Cytochrome c|Cytochrome c]]
*[[Cytochrome c|Cytochrome c]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:021267610</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Phormidium laminosum]]
[[Category: Phormidium laminosum]]
[[Category: Worrall, J A.R.]]
[[Category: Worrall, J A.R]]
[[Category: Class i cytochrome c]]
[[Category: Class i cytochrome c]]
[[Category: Cytochrome f]]
[[Category: Cytochrome f]]
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