1jvo: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1jvo |SIZE=350|CAPTION= <scene name='initialview01'>1jvo</scene>, resolution 2.75Å | |PDB= 1jvo |SIZE=350|CAPTION= <scene name='initialview01'>1jvo</scene>, resolution 2.75Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= azu ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | |GENE= azu ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1jvl|1JVL]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvo OCA], [http://www.ebi.ac.uk/pdbsum/1jvo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jvo RCSB]</span> | |||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Rossi, G L.]] | [[Category: Rossi, G L.]] | ||
[[Category: Ubbink, M.]] | [[Category: Ubbink, M.]] | ||
[[Category: covalent crosslink]] | [[Category: covalent crosslink]] | ||
[[Category: cupredoxin]] | [[Category: cupredoxin]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
''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 21:39:39 2008'' | ||
Revision as of 21:39, 30 March 2008
| |||||||
| , resolution 2.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | azu (Pseudomonas aeruginosa) | ||||||
| Related: | 1JVL
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Azurin dimer, crosslinked via disulfide bridge
OverviewOverview
The transfer of electrons between proteins is an essential step in biological energy production. Two protein redox partners are often artificially crosslinked to investigate the poorly understood mechanism by which they interact. To better understand the effect of crosslinking on electron transfer rates, we have constructed dimers of azurin by crosslinking the monomers. The measured electron exchange rates, combined with crystal structures of the dimers, demonstrate that the length of the linker can have a dramatic effect on the structure of the dimer and the electron transfer rate. The presence of ordered water molecules in the protein-protein interface may considerably influence the electronic coupling between redox centers.
About this StructureAbout this Structure
1JVO is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
ReferenceReference
Dramatic modulation of electron transfer in protein complexes by crosslinking., van Amsterdam IM, Ubbink M, Einsle O, Messerschmidt A, Merli A, Cavazzini D, Rossi GL, Canters GW, Nat Struct Biol. 2002 Jan;9(1):48-52. PMID:11740504
Page seeded by OCA on Sun Mar 30 21:39:39 2008