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New page: left|200px<br /><applet load="1mqv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mqv, resolution 1.78Å" /> '''Crystal Structure of...
 
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[[Image:1mqv.gif|left|200px]]<br /><applet load="1mqv" size="450" color="white" frame="true" align="right" spinBox="true"  
==Crystal Structure of the Q1A/F32W/W72F mutant of Rhodopseudomonas palustris cytochrome c' (prime) expressed in E. coli==
caption="1mqv, resolution 1.78&Aring;" />
<StructureSection load='1mqv' size='340' side='right' caption='[[1mqv]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
'''Crystal Structure of the Q1A/F32W/W72F mutant of Rhodopseudomonas palustris cytochrome c' (prime) expressed in E. coli'''<br />
== Structural highlights ==
<table><tr><td colspan='2'>[[1mqv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodobacillus_palustris"_molisch_1907 "rhodobacillus palustris" molisch 1907]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MQV 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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a7v|1a7v]]</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=1mqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mqv OCA], [http://pdbe.org/1mqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mqv RCSB], [http://www.ebi.ac.uk/pdbsum/1mqv PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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/initialview01.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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1MQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MQV OCA].
</div>
<div class="pdbe-citations 1mqv" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12407175 12407175]
*[[Cytochrome c|Cytochrome c]]
[[Category: Rhodopseudomonas palustris]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Engman, K.C.]]
__TOC__
[[Category: Gray, H.B.]]
</StructureSection>
[[Category: Lee, J.C.]]
[[Category: Rhodobacillus palustris molisch 1907]]
[[Category: Tezcan, F.A.]]
[[Category: Engman, K C]]
[[Category: Winkler, J.R.]]
[[Category: Gray, H B]]
[[Category: HEM]]
[[Category: Lee, J C]]
[[Category: four-helix bundle]]
[[Category: Tezcan, F A]]
 
[[Category: Winkler, J R]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:38:36 2007''
[[Category: Electron transport]]
[[Category: Four-helix bundle]]

Latest revision as of 18:36, 7 February 2016

Crystal Structure of the Q1A/F32W/W72F mutant of Rhodopseudomonas palustris cytochrome c' (prime) expressed in E. coliCrystal Structure of the Q1A/F32W/W72F mutant of Rhodopseudomonas palustris cytochrome c' (prime) expressed in E. coli

Structural highlights

1mqv is a 2 chain structure with sequence from "rhodobacillus_palustris"_molisch_1907 "rhodobacillus palustris" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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 (< 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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Lee JC, Engman KC, Tezcan FA, Gray HB, Winkler JR. Structural features of cytochrome c' folding intermediates revealed by fluorescence energy-transfer kinetics. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14778-82. Epub 2002 Oct 29. PMID:12407175 doi:10.1073/pnas.192574099

1mqv, resolution 1.78Å

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