1l5h
From Proteopedia
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|PDB= 1l5h |SIZE=350|CAPTION= <scene name='initialview01'>1l5h</scene>, resolution 2.3Å | |PDB= 1l5h |SIZE=350|CAPTION= <scene name='initialview01'>1l5h</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5h OCA], [http://www.ebi.ac.uk/pdbsum/1l5h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l5h RCSB]</span> | ||
}} | }} | ||
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[[Category: Thomas, L M.]] | [[Category: Thomas, L M.]] | ||
[[Category: Yoshida, M.]] | [[Category: Yoshida, M.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CLF]] | ||
[[Category: apo-protein]] | [[Category: apo-protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:58:22 2008'' |
Revision as of 18:58, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Nitrogenase, with EC number 1.18.6.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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