1bxu
From Proteopedia
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|PDB= 1bxu |SIZE=350|CAPTION= <scene name='initialview01'>1bxu</scene>, resolution 1.9Å | |PDB= 1bxu |SIZE=350|CAPTION= <scene name='initialview01'>1bxu</scene>, resolution 1.9Å | ||
|SITE= <scene name='pdbsite=CUB:Cu+Binding+Site'>CUB</scene> | |SITE= <scene name='pdbsite=CUB:Cu+Binding+Site'>CUB</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxu OCA], [http://www.ebi.ac.uk/pdbsum/1bxu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bxu RCSB]</span> | ||
}} | }} | ||
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[[Category: Suzuki, E.]] | [[Category: Suzuki, E.]] | ||
[[Category: Tsukui, H.]] | [[Category: Tsukui, H.]] | ||
| - | [[Category: CU]] | ||
[[Category: copper protein]] | [[Category: copper protein]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
| - | ''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 19:10:30 2008'' |
Revision as of 16:10, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Sites: | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OXIDIZED PLASTOCYANIN FROM SYNECHOCOCCUS SP.
Overview
The crystal structures of oxidized and reduced plastocyanins from Synechococcus sp. PCC 7942 have been determined at 1.9 and 1.8 A resolution, respectively, at pH 5.0. The protein consists of only 91 amino acid residues, the smallest number known for a plastocyanin, and apparently lacks the mostly conserved acidic patch that is believed to be important for recognition with electron-transfer partners. The protein has two acidic residues, Glu42 and Glu85, around Tyr83, which is thought to be a possible conduit for electrons, but these are neutralized by Arg88 and Lys58. Residue Arg88 interacts with Tyr83 through a pi-pi interaction in which the guanidinium group of the former completely overlaps the aromatic ring of the tyrosine. Reduction of the protein at pH 5.0 causes a lengthening of one Cu-N(His) bond by 0.36 A, despite the small rms deviation of 0.08 A calculated for the backbone atoms. Moreover, significant conformational changes of Arg88 and Lys58, along with the movement of a water molecule adjacent to the OH group of Tyr83, were observed on reduction; the guanidinium group of Arg88 rotates by more than 11 degrees, and the water molecule moves by 0.42 A. The changes around the copper site and the alterations around Tyr83 may be linked to the reduction of the copper.
About this Structure
1BXU is a Single protein structure of sequence from Synechococcus sp.. Full crystallographic information is available from OCA.
Reference
Crystal structure determinations of oxidized and reduced plastocyanin from the cyanobacterium Synechococcus sp. PCC 7942., Inoue T, Sugawara H, Hamanaka S, Tsukui H, Suzuki E, Kohzuma T, Kai Y, Biochemistry. 1999 May 11;38(19):6063-9. PMID:10320332
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