1all
From Proteopedia
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- | [[Image:1all.gif|left|200px]] | + | [[Image:1all.gif|left|200px]] |
- | + | ||
- | '''ALLOPHYCOCYANIN''' | + | {{Structure |
+ | |PDB= 1all |SIZE=350|CAPTION= <scene name='initialview01'>1all</scene>, resolution 2.3Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene> and <scene name='pdbligand=CH3:METHYL GROUP'>CH3</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''ALLOPHYCOCYANIN''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1ALL is a [ | + | 1ALL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALL OCA]. |
==Reference== | ==Reference== | ||
- | Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 A resolution., Brejc K, Ficner R, Huber R, Steinbacher S, J Mol Biol. 1995 Jun 2;249(2):424-40. PMID:[http:// | + | Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 A resolution., Brejc K, Ficner R, Huber R, Steinbacher S, J Mol Biol. 1995 Jun 2;249(2):424-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7783202 7783202] |
[[Category: Arthrospira platensis]] | [[Category: Arthrospira platensis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: phycobiliprotein]] | [[Category: phycobiliprotein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:16 2008'' |
Revision as of 07:59, 20 March 2008
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, resolution 2.3Å | |||||||
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Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
ALLOPHYCOCYANIN
Overview
The phycobiliprotein allophycocyanin from the cyanobacterium Spirulina platensis has been isolated and crystallized. The crystals belong to space group P6(3)22 with cell constants a = b = 101.9 A, c = 130.6 A, alpha = beta = 90 degrees, gamma = 120 degrees, with one (alpha beta) monomer in the asymmetric unit. The three-dimensional structure of the (alpha beta) monomer was solved by multiple isomorphous replacement. The crystal structure has been refined in a cyclic manner by energy-restrained crystallographic refinement and model building. The conventional crystallographic R-factor of the final model is 19.6% with data from 8.0 to 2.3 A. The molecular structure of the subunits resembles other solved phycobiliprotein structures. In comparison to C-phycocyanin and b-phycoerythrin the major differences arise from deletions and insertions of segments involved in the protein-chromophore interactions. The stereochemistry of the alpha 84 and beta 84 chiral atoms are C(2)-R, C(3)-R and C(31)-R. The configuration (C(4)-Z, C(10)-Z and C(15)-Z) and the conformation (C(5)-anti, C(9)-syn and C(14)-anti) are equal for both chromophores.
About this Structure
1ALL is a Protein complex structure of sequences from Arthrospira platensis. Full crystallographic information is available from OCA.
Reference
Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 A resolution., Brejc K, Ficner R, Huber R, Steinbacher S, J Mol Biol. 1995 Jun 2;249(2):424-40. PMID:7783202
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