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1b33

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|PDB= 1b33 |SIZE=350|CAPTION= <scene name='initialview01'>1b33</scene>, resolution 2.3&Aring;
|PDB= 1b33 |SIZE=350|CAPTION= <scene name='initialview01'>1b33</scene>, resolution 2.3&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene>, <scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene> and <scene name='pdbligand=BO4:BORATE ION'>BO4</scene>
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|LIGAND= <scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene>, <scene name='pdbligand=BO4:BORATE+ION'>BO4</scene>, <scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene>, <scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b33 OCA], [http://www.ebi.ac.uk/pdbsum/1b33 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b33 RCSB]</span>
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[[Category: Than, M E.]]
[[Category: Than, M E.]]
[[Category: Wiegand, G.]]
[[Category: Wiegand, G.]]
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[[Category: BLA]]
 
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[[Category: BO4]]
 
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[[Category: CYC]]
 
[[Category: allophycocyanin]]
[[Category: allophycocyanin]]
[[Category: complex structure]]
[[Category: complex structure]]
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[[Category: linker polypeptide]]
[[Category: linker polypeptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:05:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:52:34 2008''

Revision as of 15:52, 30 March 2008


PDB ID 1b33

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: , , ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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