2plt: Difference between revisions
New page: left|200px<br /><applet load="2plt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2plt, resolution 1.5Å" /> '''STRUCTURE DETERMINATI... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2plt.gif|left|200px]]<br /><applet load="2plt" size=" | [[Image:2plt.gif|left|200px]]<br /><applet load="2plt" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2plt, resolution 1.5Å" /> | caption="2plt, resolution 1.5Å" /> | ||
'''STRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALF'''<br /> | '''STRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALF'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of plastocyanin from the green alga Chlamydomonas | 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. | ||
==About this Structure== | ==About this Structure== | ||
2PLT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with CU and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2PLT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLT OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Merchant, S.]] | [[Category: Merchant, S.]] | ||
[[Category: Redinbo, M | [[Category: Redinbo, M R.]] | ||
[[Category: Yeates, T | [[Category: Yeates, T O.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CU]] | [[Category: CU]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:47 2008'' | ||
Revision as of 19:30, 21 February 2008
|
STRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALF
OverviewOverview
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.
About this StructureAbout this Structure
2PLT is a Single protein structure of sequence from Chlamydomonas reinhardtii with and as ligands. 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 Thu Feb 21 18:30:47 2008