1adw: Difference between revisions
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|PDB= 1adw |SIZE=350|CAPTION= <scene name='initialview01'>1adw</scene>, resolution 2.5Å | |PDB= 1adw |SIZE=350|CAPTION= <scene name='initialview01'>1adw</scene>, resolution 2.5Å | ||
|SITE= <scene name='pdbsite=CUA:Cu+Binding+Site+-+HIS+40,+CYS+78,+HIS+81,+And+MET+86+Are+...'>CUA</scene> and <scene name='pdbsite=CUB:Cu+Binding+Site+-+HIS+40,+CYS+78,+HIS+81,+And+MET+86+Are+...'>CUB</scene> | |SITE= <scene name='pdbsite=CUA:Cu+Binding+Site+-+HIS+40,+CYS+78,+HIS+81,+And+MET+86+Are+...'>CUA</scene> and <scene name='pdbsite=CUB:Cu+Binding+Site+-+HIS+40,+CYS+78,+HIS+81,+And+MET+86+Are+...'>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=1adw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adw OCA], [http://www.ebi.ac.uk/pdbsum/1adw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1adw RCSB]</span> | |||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Williams, P A.]] | [[Category: Williams, P A.]] | ||
[[Category: copper]] | [[Category: copper]] | ||
[[Category: cuproprotein]] | [[Category: cuproprotein]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
''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 18:38:07 2008'' | ||
Revision as of 18:38, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Sites: | and | ||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PSEUDOAZURIN
OverviewOverview
The structure of pseudoazurin from Thiosphaera pantotropha has been determined and compared to structures of both soluble and membrane-bound periplasmic redox proteins. The results show a matching set of unipolar, but promiscuous, docking motifs based on a positive hydrophobic surface patch on the electron shuttle proteins pseudoazurin and cytochrome c550 and a negative hydrophobic patch on the surface of their known redox partners. The observed electrostatic handedness is argued to be associated with the charge-asymmetry of the membrane-bound components of the redox chain due to von Heijne's 'positives-inside' principle. We propose a 'positives-in-between' rule for electron shuttle proteins, and expect a negative hydrophobic patch to be present on both the highest and lowest redox potential species in a series of electron carriers.
About this StructureAbout this Structure
1ADW is a Single protein structure of sequence from Paracoccus pantotrophus. Full crystallographic information is available from OCA.
ReferenceReference
Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase., Williams PA, Fulop V, Leung YC, Chan C, Moir JW, Howlett G, Ferguson SJ, Radford SE, Hajdu J, Nat Struct Biol. 1995 Nov;2(11):975-82. PMID:7583671
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