1gm4: Difference between revisions

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[[Image:1gm4.jpg|left|200px]]<br /><applet load="1gm4" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1gm4.jpg|left|200px]]
caption="1gm4, resolution 2.05&Aring;" />
 
'''OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6'''<br />
{{Structure
|PDB= 1gm4 |SIZE=350|CAPTION= <scene name='initialview01'>1gm4</scene>, resolution 2.05&Aring;
|SITE= <scene name='pdbsite=AC1:Hec+Binding+Site+For+Residue+A204'>AC1</scene>
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HEC:HEME C'>HEC</scene>
|ACTIVITY=
|GENE=
}}
 
'''OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1GM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Hec+Binding+Site+For+Residue+A204'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GM4 OCA].  
1GM4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GM4 OCA].  


==Reference==
==Reference==
Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome., Louro RO, Bento I, Matias PM, Catarino T, Baptista AM, Soares CM, Carrondo MA, Turner DL, Xavier AV, J Biol Chem. 2001 Nov 23;276(47):44044-51. Epub 2001 Sep 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11551953 11551953]
Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome., Louro RO, Bento I, Matias PM, Catarino T, Baptista AM, Soares CM, Carrondo MA, Turner DL, Xavier AV, J Biol Chem. 2001 Nov 23;276(47):44044-51. Epub 2001 Sep 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11551953 11551953]
[[Category: Desulfovibrio desulfuricans]]
[[Category: Desulfovibrio desulfuricans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: electron transport]]
[[Category: electron transport]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:36 2008''
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Revision as of 12:25, 20 March 2008

File:1gm4.jpg


PDB ID 1gm4

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, resolution 2.05Å
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Ligands: and
Coordinates: save as pdb, mmCIF, xml



OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6


OverviewOverview

Cell metabolism relies on energy transduction usually performed by complex membrane-spanning proteins that couple different chemical processes, e.g. electron and proton transfer in proton-pumps. There is great interest in determining at the molecular level the structural details that control these energy transduction events, particularly those involving multiple electrons and protons, because tight control is required to avoid the production of dangerous reactive intermediates. Tetraheme cytochrome c(3) is a small soluble and monomeric protein that performs a central step in the bioenergetic metabolism of sulfate reducing bacteria, termed "proton-thrusting," linking the oxidation of molecular hydrogen with the reduction of sulfate. The mechano-chemical coupling involved in the transfer of multiple electrons and protons in cytochrome c(3) from Desulfovibrio desulfuricans ATCC 27774 is described using results derived from the microscopic thermodynamic characterization of the redox and acid-base centers involved, crystallographic studies in the oxidized and reduced states of the cytochrome, and theoretical studies of the redox and acid-base transitions. This proton-assisted two-electron step involves very small, localized structural changes that are sufficient to generate the complex network of functional cooperativities leading to energy transduction, while using molecular mechanisms distinct from those established for other Desulfovibrio sp. cytochromes from the same structural family.

About this StructureAbout this Structure

1GM4 is a Single protein structure of sequence from Desulfovibrio desulfuricans. Full crystallographic information is available from OCA.

ReferenceReference

Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome., Louro RO, Bento I, Matias PM, Catarino T, Baptista AM, Soares CM, Carrondo MA, Turner DL, Xavier AV, J Biol Chem. 2001 Nov 23;276(47):44044-51. Epub 2001 Sep 10. PMID:11551953

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