1b33
From Proteopedia
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|PDB= 1b33 |SIZE=350|CAPTION= <scene name='initialview01'>1b33</scene>, resolution 2.3Å | |PDB= 1b33 |SIZE=350|CAPTION= <scene name='initialview01'>1b33</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene>, <scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene> | + | |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= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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.]] | ||
| - | [[Category: BLA]] | ||
| - | [[Category: BO4]] | ||
| - | [[Category: CYC]] | ||
[[Category: allophycocyanin]] | [[Category: allophycocyanin]] | ||
[[Category: complex structure]] | [[Category: complex structure]] | ||
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[[Category: linker polypeptide]] | [[Category: linker polypeptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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| , 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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