1kqg

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|PDB= 1kqg |SIZE=350|CAPTION= <scene name='initialview01'>1kqg</scene>, resolution 2.80&Aring;
|PDB= 1kqg |SIZE=350|CAPTION= <scene name='initialview01'>1kqg</scene>, resolution 2.80&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=6MO:MOLYBDENUM(VI)+ION'>6MO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HQO:2-HEPTYL-4-HYDROXY+QUINOLINE+N-OXIDE'>HQO</scene> and <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>
+
|LIGAND= <scene name='pdbligand=6MO:MOLYBDENUM(VI)+ION'>6MO</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CSE:SELENOCYSTEINE'>CSE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HQO:2-HEPTYL-4-HYDROXY+QUINOLINE+N-OXIDE'>HQO</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Formate_dehydrogenase Formate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.2 1.2.1.2]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Formate_dehydrogenase Formate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.2 1.2.1.2] </span>
|GENE=
|GENE=
 +
|DOMAIN=
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|RELATEDENTRY=[[1kqf|1KQF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kqg OCA], [http://www.ebi.ac.uk/pdbsum/1kqg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kqg RCSB]</span>
}}
}}
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[[Category: Jormakka, M.]]
[[Category: Jormakka, M.]]
[[Category: Tornroth, S.]]
[[Category: Tornroth, S.]]
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[[Category: 6MO]]
 
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[[Category: CDL]]
 
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[[Category: HEM]]
 
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[[Category: HQO]]
 
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[[Category: MGD]]
 
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[[Category: SF4]]
 
[[Category: anaerobic]]
[[Category: anaerobic]]
[[Category: dehydrogenase]]
[[Category: dehydrogenase]]
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[[Category: selenocysteine]]
[[Category: selenocysteine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:20:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:52:07 2008''

Revision as of 18:52, 30 March 2008

Image:1kqg.jpg


PDB ID 1kqg

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands: , , , , , ,
Activity: Formate dehydrogenase, with EC number 1.2.1.2
Related: 1KQF


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



FORMATE DEHYDROGENASE N FROM E. COLI


Overview

The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined at 1.6 angstroms. The structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 angstroms through the enzyme. The menaquinone reduction site associated with a possible proton pathway was also characterized. This structure provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.

About this Structure

1KQG is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Molecular basis of proton motive force generation: structure of formate dehydrogenase-N., Jormakka M, Tornroth S, Byrne B, Iwata S, Science. 2002 Mar 8;295(5561):1863-8. PMID:11884747

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