1lqu
From Proteopedia
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|PDB= 1lqu |SIZE=350|CAPTION= <scene name='initialview01'>1lqu</scene>, resolution 1.25Å | |PDB= 1lqu |SIZE=350|CAPTION= <scene name='initialview01'>1lqu</scene>, resolution 1.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0493 GltD]</span> | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqu OCA], [http://www.ebi.ac.uk/pdbsum/1lqu PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1lqu RCSB]</span> | ||
}} | }} | ||
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[[Category: Tahallah, N.]] | [[Category: Tahallah, N.]] | ||
[[Category: Zanetti, G.]] | [[Category: Zanetti, G.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: NDP]] | ||
[[Category: fad]] | [[Category: fad]] | ||
[[Category: nadph]] | [[Category: nadph]] | ||
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[[Category: tuberculosis]] | [[Category: tuberculosis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:56:13 2008'' |
Revision as of 03:56, 26 March 2008
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| , resolution 1.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Domains: | GltD | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Mycobacterium tuberculosis FprA in complex with NADPH
Overview
FprA is a mycobacterial oxidoreductase that catalyzes the transfer of reducing equivalents from NADPH to a protein acceptor. We determined the atomic resolution structure of FprA in the oxidized (1.05 A resolution) and NADPH-reduced (1.25 A resolution) forms. The comparison of these FprA structures with that of bovine adrenodoxin reductase showed no significant overall differences. Hence, these enzymes, which belong to the structural family of the disulfide oxidoreductases, are structurally conserved in very distant organisms such as mycobacteria and mammals. Despite the conservation of the overall fold, the details of the active site of FprA show some peculiar features. In the oxidized enzyme complex, the bound NADP+ exhibits a covalent modification, which has been identified as an oxygen atom linked through a carbonylic bond to the reactive C4 atom of the nicotinamide ring. Mass spectrometry has confirmed this assignment. This NADP+ derivative is likely to form by oxidation of the NADP+ adduct resulting from nucleophilic attack by an active-site water molecule. A Glu-His pair is well positioned to activate the attacking water through a mechanism analogous to that of the catalytic triad in serine proteases. The NADP+ nicotinamide ring exhibits the unusual cis conformation, which may favor derivative formation. The physiological significance of this reaction is presently unknown. However, it could assist with drug-design studies in that the modified NADP+ could serve as a lead compound for the development of specific inhibitors.
About this Structure
1LQU is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
A covalent modification of NADP+ revealed by the atomic resolution structure of FprA, a Mycobacterium tuberculosis oxidoreductase., Bossi RT, Aliverti A, Raimondi D, Fischer F, Zanetti G, Ferrari D, Tahallah N, Maier CS, Heck AJ, Rizzi M, Mattevi A, Biochemistry. 2002 Jul 16;41(28):8807-18. PMID:12102623
Page seeded by OCA on Wed Mar 26 05:56:13 2008
Categories: Mycobacterium tuberculosis | Single protein | Aliverti, A. | Bossi, R T. | Ferrari, D. | Fischer, F. | Heck, A J.R. | Maier, C S. | Mattevi, A. | Raimondi, D. | Rizzi, M. | TBSGC, TB Structural Genomics Consortium. | Tahallah, N. | Zanetti, G. | Fad | Nadph | Oxidoreductase | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc | Tuberculosis
