1jvo: Difference between revisions

Revision as of 21:01, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jvo.png

Template:STRUCTURE 1jvo

Azurin dimer, crosslinked via disulfide bridgeAzurin dimer, crosslinked via disulfide bridge

Template:ABSTRACT PUBMED 11740504

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 Tue Jul 1 21:00:59 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1jvo.gif|left|200px]]
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 {{STRUCTURE_1jvo|  PDB=1jvo  |  SCENE=  }}
-'''Azurin dimer, crosslinked via disulfide bridge'''
+===Azurin dimer, crosslinked via disulfide bridge===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11740504}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11740504 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11740504}}
 ==About this Structure==
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 [[Category: Cupredoxin]]
 [[Category: Electron transfer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:58:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 21:00:59 2008''