1gu6: Difference between revisions

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[[Image:1gu6.gif|left|200px]]<br /><applet load="1gu6" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1gu6.gif|left|200px]]
caption="1gu6, resolution 2.5&Aring;" />
 
'''STRUCTURE OF THE PERIPLASMIC CYTOCHROME C NITRITE REDUCTASE FROM ESCHERICHIA COLI'''<br />
{{Structure
|PDB= 1gu6 |SIZE=350|CAPTION= <scene name='initialview01'>1gu6</scene>, resolution 2.5&Aring;
|SITE= <scene name='pdbsite=CA1:Hec+Binding+Site+For+Chain+G'>CA1</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY=
|GENE=
}}
 
'''STRUCTURE OF THE PERIPLASMIC CYTOCHROME C NITRITE REDUCTASE FROM ESCHERICHIA COLI'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1GU6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HEC:'>HEC</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=CA1:Hec+Binding+Site+For+Chain+G'>CA1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU6 OCA].  
1GU6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU6 OCA].  


==Reference==
==Reference==
Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli., Bamford VA, Angove HC, Seward HE, Thomson AJ, Cole JA, Butt JN, Hemmings AM, Richardson DJ, Biochemistry. 2002 Mar 5;41(9):2921-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11863430 11863430]
Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli., Bamford VA, Angove HC, Seward HE, Thomson AJ, Cole JA, Butt JN, Hemmings AM, Richardson DJ, Biochemistry. 2002 Mar 5;41(9):2921-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11863430 11863430]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: periplasmic nitrite reductase]]
[[Category: periplasmic nitrite reductase]]


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Revision as of 12:27, 20 March 2008

File:1gu6.gif


PDB ID 1gu6

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, resolution 2.5Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE PERIPLASMIC CYTOCHROME C NITRITE REDUCTASE FROM ESCHERICHIA COLI


OverviewOverview

The crystal structure and spectroscopic properties of the periplasmic penta-heme cytochrome c nitrite reductase (NrfA) of Escherichia coli are presented. The structure is the first for a member of the NrfA subgroup that utilize a soluble penta-heme cytochrome, NrfB, as a redox partner. Comparison to the structures of Wolinella succinogenes NrfA and Sulfospirillum deleyianum NrfA, which accept electrons from a membrane-anchored tetra-heme cytochrome (NrfH), reveals notable differences in the protein surface around heme 2, which may be the docking site for the redox partner. The structure shows that four of the NrfA hemes (hemes 2-5) have bis-histidine axial heme-Fe ligation. The catalytic heme-Fe (heme 1) has a lysine distal ligand and an oxygen atom proximal ligand. Analysis of NrfA in solution by magnetic circular dichroism (MCD) suggested that the oxygen ligand arose from water. Electron paramagnetic resonance (EPR) spectra were collected from electrochemically poised NrfA samples. Broad perpendicular mode signals at g similar 10.8 and 3.5, characteristic of weakly spin-coupled S = 5/2, S = 1/2 paramagnets, titrated with E(m) = -107 mV. A possible origin for these are the active site Lys-OH(2) coordinated heme (heme 1) and a nearby bis-His coordinated heme (heme 3). A rhombic heme Fe(III) EPR signal at g(z) = 2.91, g(y) = 2.3, g(x) = 1.5 titrated with E(m) = -37 mV and is likely to arise from bis-His coordinated heme (heme 2) in which the interplanar angle of the imidazole rings is 21.2. The final two bis-His coordinated hemes (hemes 4 and 5) have imidazole interplanar angles of 64.4 and 71.8. Either, or both, of these hemes could give rise to a "Large g max" EPR signal at g(z)() = 3.17 that titrated at potentials between -250 and -400 mV. Previous spectroscopic studies on NrfA from a number of bacterial species are considered in the light of the structure-based spectro-potentiometric analysis presented for the E. coli NrfA.

About this StructureAbout this Structure

1GU6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli., Bamford VA, Angove HC, Seward HE, Thomson AJ, Cole JA, Butt JN, Hemmings AM, Richardson DJ, Biochemistry. 2002 Mar 5;41(9):2921-31. PMID:11863430

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