1f5v: Difference between revisions
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New page: left|200px<br /><applet load="1f5v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f5v, resolution 1.7Å" /> '''STRUCTURE AND SITE-DI... |
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[[Image:1f5v.jpg|left|200px]]<br /><applet load="1f5v" size=" | [[Image:1f5v.jpg|left|200px]]<br /><applet load="1f5v" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1f5v, resolution 1.7Å" /> | caption="1f5v, resolution 1.7Å" /> | ||
'''STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION'''<br /> | '''STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of a major oxygen-insensitive nitroreductase (NfsA) | The crystal structure of a major oxygen-insensitive nitroreductase (NfsA) from Escherichia coli has been solved by the molecular replacement method at 1.7-A resolution. This enzyme is a homodimeric flavoprotein with one FMN cofactor per monomer and catalyzes reduction of nitrocompounds using NADPH. The structure exhibits an alpha + beta-fold, and is comprised of a central domain and an excursion domain. The overall structure of NfsA is similar to the NADPH-dependent flavin reductase of Vibrio harveyi, despite definite difference in the spatial arrangement of residues around the putative substrate-binding site. On the basis of the crystal structure of NfsA and its alignment with the V. harveyi flavin reductase and the NADPH-dependent nitro/flavin reductase of Bacillus subtilis, residues Arg(203) and Arg(208) of the loop region between helices I and J in the vicinity of the catalytic center FMN is predicted as a determinant for NADPH binding. The R203A mutant results in a 33-fold increase in the K(m) value for NADPH indicating that the side chain of Arg(203) plays a key role in binding NADPH possibly to interact with the 2'-phosphate group. | ||
==About this Structure== | ==About this Structure== | ||
1F5V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/NADPH_dehydrogenase_(quinone) NADPH dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.6 1.6.99.6] Full crystallographic information is available from [http:// | 1F5V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/NADPH_dehydrogenase_(quinone) NADPH dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.6 1.6.99.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5V OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kobori, T.]] | [[Category: Kobori, T.]] | ||
[[Category: Lee, W | [[Category: Lee, W C.]] | ||
[[Category: Murphy, M | [[Category: Murphy, M E.P.]] | ||
[[Category: Saigo, K.]] | [[Category: Saigo, K.]] | ||
[[Category: Sasaki, H.]] | [[Category: Sasaki, H.]] | ||
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[[Category: oxidoreduction]] | [[Category: oxidoreduction]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:11 2008'' | ||
