2new

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 2new |SIZE=350|CAPTION= <scene name='initialview01'>2new</scene>
|PDB= 2new |SIZE=350|CAPTION= <scene name='initialview01'>2new</scene>
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene>
+
|LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2new FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2new OCA], [http://www.ebi.ac.uk/pdbsum/2new PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2new RCSB]</span>
}}
}}
Line 27: Line 30:
[[Category: Bruschi, M.]]
[[Category: Bruschi, M.]]
[[Category: Turano, P.]]
[[Category: Turano, P.]]
-
[[Category: HEC]]
 
[[Category: cytochrome]]
[[Category: cytochrome]]
[[Category: cytochrome c7]]
[[Category: cytochrome c7]]
Line 33: Line 35:
[[Category: multiheme cytochrome]]
[[Category: multiheme cytochrome]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:47:50 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:04:43 2008''

Revision as of 01:04, 31 March 2008


PDB ID 2new

Drag the structure with the mouse to rotate
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CYTOCHROME C551.5, NMR, STRUCTURES 19-35 OF 35


Overview

The solution structure of Desulfuromonas acetoxidans cytochrome c7 has been refined by using 1H-NMR spectra recorded at 800 MHz and by using pseudocontact shifts in the final energy minimization procedure. The protein, composed of 68 amino acids, contains three paramagnetic heme moieties, each with one unpaired electron. The largely distributed paramagnetism broadens the lines in several protein parts. The structure is now relatively well resolved all over the backbone by the use of 1315 meaningful NOEs and 90 pseudocontact shifts. The statistical analysis of the structure indicates its satisfactory quality. The protein-fold is quite similar to that of the analogous four-heme cytochromes c3 for those parts which can be considered homologous. The solvent accessibility and the electrostatic potential surfaces surrounding the three hemes have been analyzed in terms of their reduction potentials. The resulting magnetic susceptibility anisotropy data obtained from pseudocontact shifts are analyzed in terms of structural data.

About this Structure

2NEW is a Single protein structure of sequence from Desulfuromonas acetoxidans. Full crystallographic information is available from OCA.

Reference

800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans., Assfalg M, Banci L, Bertini I, Bruschi M, Turano P, Eur J Biochem. 1998 Sep 1;256(2):261-70. PMID:9760163

Page seeded by OCA on Mon Mar 31 04:04:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools