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[[Image:1mqv.gif|left|200px]]


{{Structure
==Crystal Structure of the Q1A/F32W/W72F mutant of Rhodopseudomonas palustris cytochrome c' (prime) expressed in E. coli==
|PDB= 1mqv |SIZE=350|CAPTION= <scene name='initialview01'>1mqv</scene>, resolution 1.78&Aring;
<StructureSection load='1mqv' size='340' side='right'caption='[[1mqv]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
<table><tr><td colspan='2'>[[1mqv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MQV FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</td></tr>
|GENE=  
<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>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqv OCA], [https://pdbe.org/1mqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mqv RCSB], [https://www.ebi.ac.uk/pdbsum/1mqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mqv ProSAT]</span></td></tr>
|RELATEDENTRY=[[1a7v|1A7V]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqv OCA], [http://www.ebi.ac.uk/pdbsum/1mqv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mqv RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CYCP_RHOPA CYCP_RHOPA] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
== 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/mq/1mqv_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=1mqv ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We employed fluorescence energy-transfer probes to investigate the polypeptide dynamics accompanying cytochrome c' folding. Analysis of fluorescence energy-transfer kinetics from wild-type Trp-72 or Trp-32 in a crystallographically characterized (1.78 A) Q1A/F32W/W72F mutant shows that there is structural heterogeneity in denatured cytochrome c'. Even at guanidine hydrochloride concentrations well beyond the unfolding transition, a substantial fraction of the polypeptides ( approximately 50%) adopts compact conformations (tryptophan-to-heme distance, approximately 25 A) in both pseudo-wild-type (Q1A) and mutant proteins. A burst phase (&lt; or =5 ms) is revealed when stopped flow-triggered refolding is probed by tryptophan intensity: measurements on the Q1A protein show that approximately 75% of the Trp-72 fluorescence (83% for Trp-32) is quenched within the mixing deadtime, suggesting that most of the polypeptides have collapsed.


'''Crystal Structure of the Q1A/F32W/W72F mutant of Rhodopseudomonas palustris cytochrome c' (prime) expressed in E. coli'''
Structural features of cytochrome c' folding intermediates revealed by fluorescence energy-transfer kinetics.,Lee JC, Engman KC, Tezcan FA, Gray HB, Winkler JR Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14778-82. Epub 2002 Oct 29. PMID:12407175<ref>PMID:12407175</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mqv" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
We employed fluorescence energy-transfer probes to investigate the polypeptide dynamics accompanying cytochrome c' folding. Analysis of fluorescence energy-transfer kinetics from wild-type Trp-72 or Trp-32 in a crystallographically characterized (1.78 A) Q1A/F32W/W72F mutant shows that there is structural heterogeneity in denatured cytochrome c'. Even at guanidine hydrochloride concentrations well beyond the unfolding transition, a substantial fraction of the polypeptides ( approximately 50%) adopts compact conformations (tryptophan-to-heme distance, approximately 25 A) in both pseudo-wild-type (Q1A) and mutant proteins. A burst phase (&lt; or =5 ms) is revealed when stopped flow-triggered refolding is probed by tryptophan intensity: measurements on the Q1A protein show that approximately 75% of the Trp-72 fluorescence (83% for Trp-32) is quenched within the mixing deadtime, suggesting that most of the polypeptides have collapsed.
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 
== References ==
==About this Structure==
<references/>
1MQV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQV OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Structural features of cytochrome c' folding intermediates revealed by fluorescence energy-transfer kinetics., Lee JC, Engman KC, Tezcan FA, Gray HB, Winkler JR, Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14778-82. Epub 2002 Oct 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12407175 12407175]
[[Category: Rhodopseudomonas palustris]]
[[Category: Rhodopseudomonas palustris]]
[[Category: Single protein]]
[[Category: Engman KC]]
[[Category: Engman, K C.]]
[[Category: Gray HB]]
[[Category: Gray, H B.]]
[[Category: Lee JC]]
[[Category: Lee, J C.]]
[[Category: Tezcan FA]]
[[Category: Tezcan, F A.]]
[[Category: Winkler JR]]
[[Category: Winkler, J R.]]
[[Category: four-helix bundle]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:19:57 2008''
Retrieved from "https://proteopedia.org/1mqv"