2dke
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2dke |SIZE=350|CAPTION= <scene name='initialview01'>2dke</scene>, resolution 2.5Å | |PDB= 2dke |SIZE=350|CAPTION= <scene name='initialview01'>2dke</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phycocyanobilin:ferredoxin_oxidoreductase Phycocyanobilin:ferredoxin oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.7.5 1.3.7.5] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phycocyanobilin:ferredoxin_oxidoreductase Phycocyanobilin:ferredoxin oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.7.5 1.3.7.5] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2d1e|2D1E]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dke OCA], [http://www.ebi.ac.uk/pdbsum/2dke PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dke RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Sugishima, M.]] | [[Category: Sugishima, M.]] | ||
[[Category: Takahashi, Y.]] | [[Category: Takahashi, Y.]] | ||
| - | [[Category: CL]] | ||
[[Category: alpha-beta-alpha sandwich]] | [[Category: alpha-beta-alpha sandwich]] | ||
[[Category: substrate free form]] | [[Category: substrate free form]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:35:45 2008'' |
Revision as of 23:35, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Phycocyanobilin:ferredoxin oxidoreductase, with EC number 1.3.7.5 | ||||||
| Related: | 2D1E
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of substrate-free form of PcyA
Overview
Phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes the sequential reduction of the vinyl group of the D-ring and the A-ring of biliverdin IXalpha (BV) using ferredoxin to produce phycocyanobilin, a pigment used for light-harvesting and light-sensing in red algae and cyanobacteria. We have determined the crystal structure of the substrate-free form of PcyA from Synechocystis sp. PCC 6803 at 2.5 A resolution. Structural comparison of the substrate-free form and the PcyA-BV complex shows major changes around the entrance of the BV binding pocket; upon BV binding, two alpha-helices and nearby side-chains move to produce tight BV binding. Unexpectedly, these movements localize the positive charges around the BV binding site, which may contribute to the proper binding of ferredoxin to PcyA. In the substrate-free form, the side-chain of Asp105 was located at a site that would be underneath the BV A-ring in the PcyA-BV complex and hydrogen-bonded with His88. We propose that BV is protonated by a mechanism involving conformational changes of these two residues before reduction.
About this Structure
2DKE is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
Reference
Induced-fitting and electrostatic potential change of PcyA upon substrate binding demonstrated by the crystal structure of the substrate-free form., Hagiwara Y, Sugishima M, Takahashi Y, Fukuyama K, FEBS Lett. 2006 Jul 10;580(16):3823-8. Epub 2006 Jun 12. PMID:16782089
Page seeded by OCA on Mon Mar 31 02:35:45 2008
