1kqf: Difference between revisions

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[[Image:1kqf.~~gif~~|left|200px]]

[[Image:1kqf.png|left|200px]]

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~~'''~~FORMATE DEHYDROGENASE N FROM E. COLI~~'''~~

===FORMATE DEHYDROGENASE N FROM E. COLI===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_11884747}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11884747 is the PubMed ID number.

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==About this Structure==

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[[Category: Selenium]]

[[Category: Selenocysteine]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 23:02:46 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:46:16 2008''

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-[[Image:1kqf.gif|left|200px]]
+{{Seed}}
+[[Image:1kqf.png|left|200px]]
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 {{STRUCTURE_1kqf|  PDB=1kqf  |  SCENE=  }}
-'''FORMATE DEHYDROGENASE N FROM E. COLI'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11884747}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11884747 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11884747}}
 ==About this Structure==
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 [[Category: Selenium]]
 [[Category: Selenocysteine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:02:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:46:16 2008''