2nip

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(New page: 200px<br /> <applet load="2nip" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nip, resolution 2.2&Aring;" /> '''NITROGENASE IRON PRO...)
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==About this Structure==
==About this Structure==
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2NIP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]] 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=2NIP OCA]].
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2NIP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]] 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: FS4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NIP 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: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
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[[Category: Nitrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chakrabarti, P.]]
[[Category: Chakrabarti, P.]]
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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 20:31:16 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:22:14 2007''

Revision as of 11:17, 30 October 2007


2nip, resolution 2.2Å

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NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII

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

2NIP is a [Single protein] structure of sequence from [Azotobacter vinelandii] with SF4 as [ligand]. Active as [Nitrogenase], with EC number [1.18.6.1]. Structure known Active Site: FS4. 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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