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1kqg

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Revision as of 00:21, 10 September 2015

FORMATE DEHYDROGENASE N FROM E. COLI

Structural highlights

1kqg is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Related:	1kqf
Activity:	Formate dehydrogenase, with EC number 1.2.1.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[FDNG_ECOLI] Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).^[1] [FDNI_ECOLI] Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).^[2] [FDNH_ECOLI] Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jormakka M, Tornroth S, Byrne B, Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. PMID:11884747 doi:10.1126/science.1068186
↑ Jormakka M, Tornroth S, Byrne B, Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. PMID:11884747 doi:10.1126/science.1068186
↑ Jormakka M, Tornroth S, Byrne B, Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. PMID:11884747 doi:10.1126/science.1068186
↑ Jormakka M, Tornroth S, Byrne B, Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. PMID:11884747 doi:10.1126/science.1068186

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kqg"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kqf|1kqf]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1kqg RCSB], [http://www.ebi.ac.uk/pdbsum/1kqg PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1kqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kqg RCSB], [http://www.ebi.ac.uk/pdbsum/1kqg PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1kqg" style="background-color:#fffaf0;"></div>
 ==See Also==

1kqg

From Proteopedia

Revision as of 00:21, 10 September 2015

FORMATE DEHYDROGENASE N FROM E. COLI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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