1b33: Difference between revisions

Revision as of 12:50, 21 February 2008

STRUCTURE OF LIGHT HARVESTING COMPLEX OF ALLOPHYCOCYANIN ALPHA AND BETA CHAINS/CORE-LINKER COMPLEX AP*LC7.8

OverviewOverview

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 StructureAbout this Structure

1B33 is a Protein complex structure of sequences from Mastigocladus laminosus with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-[[Image:1b33.gif|left|200px]]<br /><applet load="1b33" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1b33.gif|left|200px]]<br /><applet load="1b33" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1b33, resolution 2.3&Aring;" />
 '''STRUCTURE OF LIGHT HARVESTING COMPLEX OF ALLOPHYCOCYANIN ALPHA AND BETA CHAINS/CORE-LINKER COMPLEX AP*LC7.8'''<br />
 ==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.
+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==
-B33 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B33 OCA].
+B33 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==
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 [[Category: Huber, R.]]
 [[Category: Reuter, W.]]
-[[Category: Than, M.E.]]
+[[Category: Than, M E.]]
 [[Category: Wiegand, G.]]
 [[Category: BLA]]
@@ Line 26: / Line 26: @@
 [[Category: linker polypeptides]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:19:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:55 2008''