1oow: Difference between revisions

Revision as of 12:52, 28 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:1oow.png

Template:STRUCTURE 1oow

The crystal structure of the spinach plastocyanin double mutant G8D/L12E gives insight into its low reactivity towards photosystem 1 and cytochrome fThe crystal structure of the spinach plastocyanin double mutant G8D/L12E gives insight into its low reactivity towards photosystem 1 and cytochrome f

Template:ABSTRACT PUBMED 14670610

About this StructureAbout this Structure

1OOW is a Single protein structure of sequence from Spinacia oleracea. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the spinach plastocyanin double mutant G8D/L12E gives insight into its low reactivity towards photosystem 1 and cytochrome f., Jansson H, Okvist M, Jacobson F, Ejdeback M, Hansson O, Sjolin L, Biochim Biophys Acta. 2003 Dec 8;1607(2-3):203-10. PMID:14670610

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

OCA

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-'''The crystal structure of the spinach plastocyanin double mutant G8D/L12E gives insight into its low reactivity towards photosystem 1 and cytochrome f'''
+===The crystal structure of the spinach plastocyanin double mutant G8D/L12E gives insight into its low reactivity towards photosystem 1 and cytochrome f===
-==Overview==
+<!--
-Plastocyanin (Pc) is a copper-containing protein, which functions as an electron carrier between the cytochrome b(6)f and photosystem 1 (PS1) complexes in the photosynthetic electron transfer (ET) chain. The ET is mediated by His87 situated in the hydrophobic surface in the north region of Pc. Also situated in this region is Leu12, which mutated to other amino acids severely disturbs the ET from cytochrome f and to PS1, indicating the importance of the hydrophobic surface. The crystal structure of the Pc double mutant G8D/L12E has been determined to 2.0 A resolution, with a crystallographic R-factor of 18.3% (R(free)=23.2%). A comparison with the wild-type structure reveals that structural differences are limited to the sites of the mutations. In particular, there is a small but significant change in the hydrophobic surface close to His87. Evidently, this leads to a mismatch in the reactive complex with the redox partners. For PS1 this results in a 20 times weaker binding and an eightfold slower ET as determined by kinetic measurements. The mutations that have been introduced do not affect the optical absorption spectrum. However, there is a small change in the EPR spectrum, which can be related to changes in the copper coordination geometry.
+The line below this paragraph, {{ABSTRACT_PUBMED_14670610}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14670610 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14670610}}
 ==About this Structure==
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 [[Category: Beta sandwich]]
 [[Category: Cupredoxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:06:44 2008''
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