1l5h
From Proteopedia
(New page: 200px<br /><applet load="1l5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l5h, resolution 2.3Å" /> '''FeMo-cofactor Deficie...) |
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| - | [[Image:1l5h.jpg|left|200px]]<br /><applet load="1l5h" size=" | + | [[Image:1l5h.jpg|left|200px]]<br /><applet load="1l5h" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l5h, resolution 2.3Å" /> | caption="1l5h, resolution 2.3Å" /> | ||
'''FeMo-cofactor Deficient Nitrogenase MoFe Protein'''<br /> | '''FeMo-cofactor Deficient Nitrogenase MoFe Protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | One of the most complex biosynthetic processes in metallobiochemistry is | + | One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous alpha and beta subunits. In this structure, one of the three alpha subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor. |
==About this Structure== | ==About this Structure== | ||
| - | 1L5H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with CA and CLF as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http:// | + | 1L5H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CLF:'>CLF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nitrogenase]] | [[Category: Nitrogenase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Burgess, B | + | [[Category: Burgess, B K.]] |
| - | [[Category: Dean, D | + | [[Category: Dean, D R.]] |
[[Category: Einsle, O.]] | [[Category: Einsle, O.]] | ||
| - | [[Category: Rees, D | + | [[Category: Rees, D C.]] |
| - | [[Category: Ribbe, M | + | [[Category: Ribbe, M W.]] |
[[Category: Schmid, B.]] | [[Category: Schmid, B.]] | ||
| - | [[Category: Thomas, L | + | [[Category: Thomas, L M.]] |
[[Category: Yoshida, M.]] | [[Category: Yoshida, M.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: apo-protein]] | [[Category: apo-protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:30 2008'' |
Revision as of 11:41, 21 February 2008
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FeMo-cofactor Deficient Nitrogenase MoFe Protein
Overview
One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous alpha and beta subunits. In this structure, one of the three alpha subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor.
About this Structure
1L5H is a Protein complex structure of sequences from Azotobacter vinelandii with and as ligands. Active as Nitrogenase, with EC number 1.18.6.1 Full crystallographic information is available from OCA.
Reference
Structure of a cofactor-deficient nitrogenase MoFe protein., Schmid B, Ribbe MW, Einsle O, Yoshida M, Thomas LM, Dean DR, Rees DC, Burgess BK, Science. 2002 Apr 12;296(5566):352-6. PMID:11951047
Page seeded by OCA on Thu Feb 21 13:41:30 2008
Categories: Azotobacter vinelandii | Nitrogenase | Protein complex | Burgess, B K. | Dean, D R. | Einsle, O. | Rees, D C. | Ribbe, M W. | Schmid, B. | Thomas, L M. | Yoshida, M. | CA | CLF | Apo-protein
