2plt: Difference between revisions

Revision as of 13:11, 27 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:2plt.png

Template:STRUCTURE 2plt

STRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALFSTRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALF

Template:ABSTRACT PUBMED 8399201

About this StructureAbout this Structure

2PLT is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

ReferenceReference

The 1.5-A crystal structure of plastocyanin from the green alga Chlamydomonas reinhardtii., Redinbo MR, Cascio D, Choukair MK, Rice D, Merchant S, Yeates TO, Biochemistry. 1993 Oct 12;32(40):10560-7. PMID:8399201

Page seeded by OCA on Sun Jul 27 13:11:06 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2plt.gif|left|200px]]
+{{Seed}}
+[[Image:2plt.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2plt|  PDB=2plt  |  SCENE=  }}
-'''STRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALF'''
+===STRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALF===
-==Overview==
+<!--
-The crystal structure of plastocyanin from the green alga Chlamydomonas reinhardtii has been determined at 1.5-A resolution with a crystallographic R factor of 16.8%. Plastocyanin is a small (98 amino acids), blue copper-binding protein that catalyzes the transfer of electrons in oxygenic photosynthesis from cytochrome f in the quinol oxidase complex to P700+ in photosystem I. Chlamydomonas reinhardtii plastocyanin is an eight-stranded, antiparallel beta-barrel with a single copper atom coordinated in quasitetrahedral geometry by two imidazole nitrogens (from His-37 and His-87), a cysteine sulfur (from Cys-84), and a methionine sulfur (from Met-92). The molecule contains a region of negative charge surrounding Tyr-83 (the putative distant site of electron transfer) and an exclusively hydrophobic region surrounding His-87; these regions are thought to be involved in the recognition of reaction partners for the purpose of directing electron transfer. Chlamydomonas reinhardtii plastocyanin is similar to the other plastocyanins of known structure, particularly the green algal plastocyanins from Enteromorpha prolifera and Scenedesmus obliquus. A potential "through-bond" path of electron transfer has been identified in the protein that involves the side chain of Tyr-83, the main-chain atoms between residues 83 and 84, the side chain of Cys-84, the copper atom, and the side chain of His-87.
+The line below this paragraph, {{ABSTRACT_PUBMED_8399201}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8399201 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8399201}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Yeates, T O.]]
 [[Category: Electron transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:22:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:11:06 2008''