From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1iuz.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1iuz.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1iuz| PDB=1iuz | SCENE= }} | | {{STRUCTURE_1iuz| PDB=1iuz | SCENE= }} |
| | | | |
| - | '''PLASTOCYANIN'''
| + | ===PLASTOCYANIN=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The crystal structure of plastocyanin from a green alga, Ulva pertusa, has been determined at 1.6-A resolution. At its copper site, U. pertusa plastocyanin has a distorted tetrahedral coordination geometry similar to other plastocyanins. In comparison with structures of plastocyanins reported formerly, a Cu(II)-Sdelta(Met92) bond distance (2.69 A) is shorter by about 0.2 A and a Cu(II)-Sgamma(Cys84) distance is longer by less than 0.1 A in U. pertusa plastocyanin. These subtle but significant differences are caused by the structural change at a His-Met loop (His87-Met92) due to an absence of a O(Asp85)-Ogamma(Ser88) hydrogen bond which is found in Enteromorpha prolifera plastocyanin. In addition, poplar and Chlamydomonas reinhardtii plastocyanins with a glutamine at residue 88 have a weak cation-pi interaction with Tyr83. This interaction lengthens the Cu(II)-Sdelta(Met92) bond of poplar and C. reinhardtii plastocyanins by 0.14 and 0.20 A, respectively. As a result of structural differences, U. pertusa plastocyanin has a less distorted geometry than the other plastocyanins. Thus, the cupric geometry is finely tuned by the interactions between residues 85 and 88 and between residues 83 and 88. This result implies that the copper site is more flexible than reported formerly and that the rack mechanism would be preferable to the entatic theory. The His-Met loop may regulate the electron transfer rate within the complex between plastocyanin and cytochrome f. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9933621}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9933621 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9933621}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 24: |
Line 28: |
| | [[Category: Shibata, N.]] | | [[Category: Shibata, N.]] |
| | [[Category: Electron transport]] | | [[Category: Electron transport]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:27:07 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:02:47 2008'' |
Revision as of 11:02, 1 July 2008
Template:STRUCTURE 1iuz
PLASTOCYANIN
Template:ABSTRACT PUBMED 9933621
About this Structure
1IUZ is a Single protein structure of sequence from Ulva pertusa. Full crystallographic information is available from OCA.
Reference
Novel insight into the copper-ligand geometry in the crystal structure of Ulva pertusa plastocyanin at 1.6-A resolution. Structural basis for regulation of the copper site by residue 88., Shibata N, Inoue T, Nagano C, Nishio N, Kohzuma T, Onodera K, Yoshizaki F, Sugimura Y, Kai Y, J Biol Chem. 1999 Feb 12;274(7):4225-30. PMID:9933621
Page seeded by OCA on Tue Jul 1 14:02:47 2008
