1h1l
From Proteopedia
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| - | [[Image:1h1l.jpg|left|200px]] | + | [[Image:1h1l.jpg|left|200px]] |
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| - | '''NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT''' | + | {{Structure |
| + | |PDB= 1h1l |SIZE=350|CAPTION= <scene name='initialview01'>1h1l</scene>, resolution 1.90Å | ||
| + | |SITE= <scene name='pdbsite=CT1:Clf+Binding+Site+For+Chain+D'>CT1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CFM:FE-MO-S+CLUSTER'>CFM</scene> and <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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H1L is a [ | + | 1H1L is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1L OCA]. |
==Reference== | ==Reference== | ||
| - | Crystallographic analysis of the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae identifies citrate as a ligand to the molybdenum of iron molybdenum cofactor (FeMoco)., Mayer SM, Gormal CA, Smith BE, Lawson DM, J Biol Chem. 2002 Sep 20;277(38):35263-6. Epub 2002 Jul 19. PMID:[http:// | + | Crystallographic analysis of the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae identifies citrate as a ligand to the molybdenum of iron molybdenum cofactor (FeMoco)., Mayer SM, Gormal CA, Smith BE, Lawson DM, J Biol Chem. 2002 Sep 20;277(38):35263-6. Epub 2002 Jul 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12133839 12133839] |
[[Category: Klebsiella pneumoniae]] | [[Category: Klebsiella pneumoniae]] | ||
[[Category: Nitrogenase]] | [[Category: Nitrogenase]] | ||
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[[Category: biological nitrogen fixation]] | [[Category: biological nitrogen fixation]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
| - | [[Category: | + | [[Category: molybdoenzyme]] |
[[Category: nitrogen metabolism]] | [[Category: nitrogen metabolism]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:30:54 2008'' |
Revision as of 09:30, 20 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , and | ||||||
| Activity: | Nitrogenase, with EC number 1.18.6.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NITROGENASE MO-FE PROTEIN FROM KLEBSIELLA PNEUMONIAE, NIFV MUTANT
Overview
The x-ray crystal structure of NifV(-) Klebsiella pneumoniae nitrogenase MoFe protein (NifV(-) Kp1) has been determined and refined to a resolution of 1.9 A. This is the first structure for a nitrogenase MoFe protein with an altered cofactor. Moreover, it is the first direct evidence that the organic acid citrate is not just present, but replaces homocitrate as a ligand to the molybdenum atom of the iron molybdenum cofactor (FeMoco). Subsequent refinement of the structure revealed that the citrate was present at reduced occupancy.
About this Structure
1H1L is a Protein complex structure of sequences from Klebsiella pneumoniae. Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae identifies citrate as a ligand to the molybdenum of iron molybdenum cofactor (FeMoco)., Mayer SM, Gormal CA, Smith BE, Lawson DM, J Biol Chem. 2002 Sep 20;277(38):35263-6. Epub 2002 Jul 19. PMID:12133839
Page seeded by OCA on Thu Mar 20 11:30:54 2008
