1cp2

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(New page: 200px<br /> <applet load="1cp2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cp2, resolution 1.93&Aring;" /> '''NITROGENASE IRON PR...)
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==About this Structure==
==About this Structure==
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1CP2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]] with SF4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CP2 OCA]].
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1CP2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]] with SF4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1]]. Structure known Active Site: FES. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CP2 OCA]].
==Reference==
==Reference==
Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum., Schlessman JL, Woo D, Joshua-Tor L, Howard JB, Rees DC, J Mol Biol. 1998 Jul 24;280(4):669-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9677296 9677296]
Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum., Schlessman JL, Woo D, Joshua-Tor L, Howard JB, Rees DC, J Mol Biol. 1998 Jul 24;280(4):669-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9677296 9677296]
[[Category: Clostridium pasteurianum]]
[[Category: Clostridium pasteurianum]]
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[[Category: Nitrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Howard, J.B.]]
[[Category: Howard, J.B.]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:40:02 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:59:35 2007''

Revision as of 09:54, 30 October 2007


1cp2, resolution 1.93Å

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NITROGENASE IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM

Overview

The nitrogenase iron (Fe) protein performs multiple functions during, biological nitrogen fixation, including mediating the mechanistically, essential coupling between ATP hydrolysis and electron transfer to the, nitrogenase molybdenum iron (MoFe) protein during substrate reduction, and, participating in the biosynthesis and insertion of the FeMo-cofactor into, the MoFe-protein. To establish a structural framework for addressing the, diverse functions of Fe-protein, crystal structures of the Fe-proteins, from Azotobacter vinelandii and Clostridium pasteurianum have been, determined at resolutions of 2.2 A and 1.93 A, respectively. These two, Fe-proteins are among the more diverse in terms of amino acid sequence and, biochemical properties. As described initially for the A. vinelandii, ... [(full description)]

About this Structure

1CP2 is a [Single protein] structure of sequence from [Clostridium pasteurianum] with SF4 as [ligand]. Active as [Nitrogenase], with EC number [1.18.6.1]. Structure known Active Site: FES. Full crystallographic information is available from [OCA].

Reference

Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum., Schlessman JL, Woo D, Joshua-Tor L, Howard JB, Rees DC, J Mol Biol. 1998 Jul 24;280(4):669-85. PMID:9677296

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