This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1b33
From Proteopedia
(New page: 200px<br /><applet load="1b33" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b33, resolution 2.3Å" /> '''STRUCTURE OF LIGHT HA...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1b33.gif|left|200px]]<br /><applet load="1b33" size=" | + | [[Image:1b33.gif|left|200px]]<br /><applet load="1b33" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b33, resolution 2.3Å" /> | caption="1b33, resolution 2.3Å" /> | ||
'''STRUCTURE OF LIGHT HARVESTING COMPLEX OF ALLOPHYCOCYANIN ALPHA AND BETA CHAINS/CORE-LINKER COMPLEX AP*LC7.8'''<br /> | '''STRUCTURE OF LIGHT HARVESTING COMPLEX OF ALLOPHYCOCYANIN ALPHA AND BETA CHAINS/CORE-LINKER COMPLEX AP*LC7.8'''<br /> | ||
==Overview== | ==Overview== | ||
| - | An electrophoretically purified allophycocyanin-linker complex, AP. LC7.8, from phycobilisomes of Mastigocladus laminosus has been crystallized in | + | An electrophoretically purified allophycocyanin-linker complex, AP. LC7.8, from phycobilisomes of Mastigocladus laminosus has been crystallized in the orthorhombic space group P212121. Cryocrystallographic x-ray measurements enabled the structural analysis of the complex at a resolution of 2.2 A. The asymmetric unit contains two side-to-side associated "trimeric" (alphabeta)3 allophycocyanin complexes comprising the linker polypeptide in a defined orientation inside the trimer. The linker representing a protein fold related to the prosegment of procarboxypeptidase A is in contact with only two of the three beta-subunits and directly interacts with the corresponding chromophores of these proteins. In addition to a modulation of the chromophores' spectral properties, the linker polypeptide attracts the alphabeta-subcomplexes, thereby bringing the beta-chromophores closer together. These results will enable interpretations of energy-transfer mechanisms within phycobiliproteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1B33 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mastigocladus_laminosus Mastigocladus laminosus] with BLA, CYC and BO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1B33 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mastigocladus_laminosus Mastigocladus laminosus] with <scene name='pdbligand=BLA:'>BLA</scene>, <scene name='pdbligand=CYC:'>CYC</scene> and <scene name='pdbligand=BO4:'>BO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B33 OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Reuter, W.]] | [[Category: Reuter, W.]] | ||
| - | [[Category: Than, M | + | [[Category: Than, M E.]] |
[[Category: Wiegand, G.]] | [[Category: Wiegand, G.]] | ||
[[Category: BLA]] | [[Category: BLA]] | ||
| Line 26: | Line 26: | ||
[[Category: linker polypeptides]] | [[Category: linker polypeptides]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:55 2008'' |
Revision as of 09:50, 21 February 2008
|
STRUCTURE OF LIGHT HARVESTING COMPLEX OF ALLOPHYCOCYANIN ALPHA AND BETA CHAINS/CORE-LINKER COMPLEX AP*LC7.8
Overview
An electrophoretically purified allophycocyanin-linker complex, AP. LC7.8, from phycobilisomes of Mastigocladus laminosus has been crystallized in the orthorhombic space group P212121. Cryocrystallographic x-ray measurements enabled the structural analysis of the complex at a resolution of 2.2 A. The asymmetric unit contains two side-to-side associated "trimeric" (alphabeta)3 allophycocyanin complexes comprising the linker polypeptide in a defined orientation inside the trimer. The linker representing a protein fold related to the prosegment of procarboxypeptidase A is in contact with only two of the three beta-subunits and directly interacts with the corresponding chromophores of these proteins. In addition to a modulation of the chromophores' spectral properties, the linker polypeptide attracts the alphabeta-subcomplexes, thereby bringing the beta-chromophores closer together. These results will enable interpretations of energy-transfer mechanisms within phycobiliproteins.
About this Structure
1B33 is a Protein complex structure of sequences from Mastigocladus laminosus with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus., Reuter W, Wiegand G, Huber R, Than ME, Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1363-8. PMID:9990029
Page seeded by OCA on Thu Feb 21 11:50:55 2008
