1mqv
From Proteopedia
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|PDB= 1mqv |SIZE=350|CAPTION= <scene name='initialview01'>1mqv</scene>, resolution 1.78Å | |PDB= 1mqv |SIZE=350|CAPTION= <scene name='initialview01'>1mqv</scene>, resolution 1.78Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1a7v|1A7V]] | ||
| + | |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> | ||
}} | }} | ||
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[[Category: Tezcan, F A.]] | [[Category: Tezcan, F A.]] | ||
[[Category: Winkler, J R.]] | [[Category: Winkler, J R.]] | ||
| - | [[Category: HEM]] | ||
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:19:57 2008'' |
Revision as of 19:19, 30 March 2008
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| , resolution 1.78Å | |||||||
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| Ligands: | |||||||
| Related: | 1A7V
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Q1A/F32W/W72F mutant of Rhodopseudomonas palustris cytochrome c' (prime) expressed in E. coli
Overview
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.
About this Structure
1MQV is a Single protein structure of sequence from Rhodopseudomonas palustris. Full crystallographic information is available from OCA.
Reference
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
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