1cje
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1cje.gif|left|200px]] | [[Image:1cje.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1cje", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | | | + | {{STRUCTURE_1cje| PDB=1cje | SCENE= }} |
- | | | + | |
- | + | ||
- | }} | + | |
'''ADRENODOXIN FROM BOVINE''' | '''ADRENODOXIN FROM BOVINE''' | ||
Line 30: | Line 27: | ||
[[Category: Waterman, M R.]] | [[Category: Waterman, M R.]] | ||
[[Category: 2fe-2s ferredoxin]] | [[Category: 2fe-2s ferredoxin]] | ||
- | [[Category: | + | [[Category: Electron transport protein]] |
- | [[Category: | + | [[Category: Iron sulfur protein]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:47:52 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 09:47, 2 May 2008
ADRENODOXIN FROM BOVINE
Overview
The three-dimensional X-ray crystal structure of full-length oxidized bovine adrenodoxin (Adx) has been determined at 2.5 A resolution by molecular replacement using a structure of a truncated form as a starting model. Crystals of Adx belong to a primitive monoclinic space group P2(1) with four Adx molecules in an asymmetric unit. The unit cell dimensions are a = 59.44 A, b = 77.03 A, c = 59.68 A, and beta = 94.83 degrees. The structure has been refined to an R factor of 23.5%. Structures of the four molecules of full-length Adx (127 amino acids) in the asymmetric unit were compared with each other and also with that of the truncated Adx (4-108). The overall topology of full-length Adx remains the same as described earlier for the truncated protein. Differences that do occur are almost wholly confined to alternate side-chain conformations that reflect differing lattice contacts made by two proteins. Extensive interactions found between molecules 1 and 2 in the full-length Adx asymmetric unit may reflect the ability of Adx to form dimers in vivo and are consistent with hydrodynamic measurements which show that in solution there is an equilibrium between monomeric and dimeric forms of Adx. Dimerization of Adx could explain why the truncated form has greater affinity for the P450 redox partner than the full-length form. From these results it can be considered that the mechanism of electron transfer is not necessarily the same in different mitochondrial P450 systems.
About this Structure
1CJE is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The tertiary structure of full-length bovine adrenodoxin suggests functional dimers., Pikuleva IA, Tesh K, Waterman MR, Kim Y, Arch Biochem Biophys. 2000 Jan 1;373(1):44-55. PMID:10620322 Page seeded by OCA on Fri May 2 12:47:52 2008