2bii: Difference between revisions
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|PDB= 2bii |SIZE=350|CAPTION= <scene name='initialview01'>2bii</scene>, resolution 1.70Å | |PDB= 2bii |SIZE=350|CAPTION= <scene name='initialview01'>2bii</scene>, resolution 1.70Å | ||
|SITE= <scene name='pdbsite=AC1:Mtv+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mtv+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MTV:(MOLYBDOPTERIN-S,S)-DIOXO-THIO-MOLYBDENUM(IV)'>MTV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Nitrate_reductase_(NAD(P)H) Nitrate reductase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.2 1.7.1.2] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrate_reductase_(NAD(P)H) Nitrate reductase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.2 1.7.1.2] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bii OCA], [http://www.ebi.ac.uk/pdbsum/2bii PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bii RCSB]</span> | |||
}} | }} | ||
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[[Category: Mendel, R R.]] | [[Category: Mendel, R R.]] | ||
[[Category: Schwarz, G.]] | [[Category: Schwarz, G.]] | ||
[[Category: fad]] | [[Category: fad]] | ||
[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:06:55 2008'' | ||
Revision as of 02:06, 31 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Nitrate reductase (NAD(P)H), with EC number 1.7.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF NITRATE-REDUCING FRAGMENT OF ASSIMILATORY NITRATE REDUCTASE FROM PICHIA ANGUSTA
OverviewOverview
Nitrate assimilation in autotrophs provides most of the reduced nitrogen on earth. In eukaryotes, reduction of nitrate to nitrite is catalyzed by the molybdenum-containing NAD(P)H:nitrate reductase (NR; EC 1.7.1.1-3). In addition to the molybdenum center, NR contains iron-heme and flavin adenine dinucleotide as redox cofactors involved in an internal electron transport chain from NAD(P)H to nitrate. Recombinant, catalytically active Pichia angusta nitrate-reducing, molybdenum-containing fragment (NR-Mo) was expressed in P. pastoris and purified. Crystal structures for NR-Mo were determined at 1.7 and 2.6 angstroms. These structures revealed a unique slot for binding nitrate in the active site and identified key Arg and Trp residues potentially involved in nitrate binding. Dimeric NR-Mo is similar in overall structure to sulfite oxidases, with significant differences in the active site. Sulfate bound in the active site caused conformational changes, as compared with the unbound enzyme. Four ordered water molecules located in close proximity to Mo define a nitrate binding site, a penta-coordinated reaction intermediate, and product release. Because yeast NAD(P)H:NR is representative of the family of eukaryotic NR, we propose a general mechanism for nitrate reduction catalysis.
About this StructureAbout this Structure
2BII is a Single protein structure of sequence from Pichia angusta. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of eukaryotic nitrate reduction: crystal structures of the nitrate reductase active site., Fischer K, Barbier GG, Hecht HJ, Mendel RR, Campbell WH, Schwarz G, Plant Cell. 2005 Apr;17(4):1167-79. Epub 2005 Mar 16. PMID:15772287
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