This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2exv

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of the F7A mutant of the cytochrome c551 from Pseudomonas aeruginosa

Structural highlights

2exv is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	351c, 1dvv, 1ynr
Gene:	nirM ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CY551_PSEAE] Electron donor for cytochrome cd1 in nitrite and nitrate respiration.

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

Several investigators have highlighted a correlation between the basic features of the folding process of a protein and its topology, which dictates the folding pathway. Within this conceptual framework we proposed that different members of the cytochrome c (cyt c) family share the same folding mechanism, involving a consensus partially structured state. Pseudomonas aeruginosa cyt c(551) (Pa cyt c(551)) folds via an apparent two-state mechanism through a high energy intermediate. Here we present kinetic evidence demonstrating that it is possible to switch its folding mechanism from two to three state, stabilizing the high energy intermediate by rational mutagenesis. Characterization of the folding kinetics of one single-site mutant of the Pa cyt c(551) (Phe(7) to Ala) indeed reveals an additional refolding phase and a fast unfolding process which are explained by the accumulation of a partially folded species. Further kinetic analysis highlights the presence of two parallel processes both leading to the native state, suggesting that the above mentioned species is a non obligatory on-pathway intermediate. Determination of the crystallographic structure of F7A shows the presence of an extended internal cavity, which hosts three "bound" water molecules and a H-bond in the N-terminal helix, which is shorter than in the wild type protein. These two features allow us to propose a detailed structural interpretation for the stabilization of the native and especially the intermediate states induced by a single crucial mutation. These results show how protein engineering, x-ray crystallography and state-of-the-art kinetics concur to unveil a folding intermediate and the structural determinants of its stability.

Unveiling a hidden folding intermediate in c-type cytochromes by protein engineering.,Borgia A, Bonivento D, Travaglini-Allocatelli C, Di Matteo A, Brunori M J Biol Chem. 2006 Apr 7;281(14):9331-6. Epub 2006 Feb 1. PMID:16452476^[1]

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

References

↑ Borgia A, Bonivento D, Travaglini-Allocatelli C, Di Matteo A, Brunori M. Unveiling a hidden folding intermediate in c-type cytochromes by protein engineering. J Biol Chem. 2006 Apr 7;281(14):9331-6. Epub 2006 Feb 1. PMID:16452476 doi:10.1074/jbc.M512127200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2exv"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the F7A mutant of the cytochrome c551 from Pseudomonas aeruginosa==
-<StructureSection load='2exv' size='340' side='right' caption='[[2exv]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
+<StructureSection load='2exv' size='340' side='right'caption='[[2exv]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2exv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EXV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2exv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EXV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[351c|351c]], [[1dvv|1dvv]], [[1ynr|1ynr]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[351c|351c]], [[1dvv|1dvv]], [[1ynr|1ynr]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nirM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nirM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=2exv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2exv OCA], [http://pdbe.org/2exv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2exv RCSB], [http://www.ebi.ac.uk/pdbsum/2exv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2exv ProSAT]</span></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=2exv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2exv OCA], [https://pdbe.org/2exv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2exv RCSB], [https://www.ebi.ac.uk/pdbsum/2exv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2exv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CY551_PSEAE CY551_PSEAE]] Electron donor for cytochrome cd1 in nitrite and nitrate respiration.
+[[https://www.uniprot.org/uniprot/CY551_PSEAE CY551_PSEAE]] Electron donor for cytochrome cd1 in nitrite and nitrate respiration.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Cytochrome c|Cytochrome c]]
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Bonivento, D]]
 [[Category: Borgia, A]]

2exv

From Proteopedia

Current revision

Crystal structure of the F7A mutant of the cytochrome c551 from Pseudomonas aeruginosa

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox