2c12: Difference between revisions
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[[Image:2c12.gif|left|200px]]<br /><applet load="2c12" size=" | [[Image:2c12.gif|left|200px]]<br /><applet load="2c12" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2c12, resolution 2.07Å" /> | caption="2c12, resolution 2.07Å" /> | ||
'''CRYSTAL STRUCTURE OF NITROALKANE OXIDASE IN COMPLEX WITH SPERMINE, A COMPETITIVE INHIBITOR'''<br /> | '''CRYSTAL STRUCTURE OF NITROALKANE OXIDASE IN COMPLEX WITH SPERMINE, A COMPETITIVE INHIBITOR'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2C12 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with SPM, FAD, PE4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Pe4 Binding Site For Chain F'>AC1</scene>. Full crystallographic information is available from [http:// | 2C12 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with <scene name='pdbligand=SPM:'>SPM</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=PE4:'>PE4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Pe4+Binding+Site+For+Chain+F'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C12 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: nitroalkane]] | [[Category: nitroalkane]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:30:08 2008'' | ||
Revision as of 11:30, 3 February 2008
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CRYSTAL STRUCTURE OF NITROALKANE OXIDASE IN COMPLEX WITH SPERMINE, A COMPETITIVE INHIBITOR
OverviewOverview
Nitroalkane oxidase (NAO) from Fusarium oxysporum catalyzes the oxidation, of neutral nitroalkanes to the corresponding aldehydes or ketones with the, production of H(2)O(2) and nitrite. The flavoenzyme is a new member of the, acyl-CoA dehydrogenase (ACAD) family, but it does not react with acyl-CoA, substrates. We present the 2.2 A resolution crystal structure of NAO, trapped during the turnover of nitroethane as a covalent N5-FAD adduct, (ES*). The homotetrameric structure of ES* was solved by MAD phasing with, 52 Se-Met sites in an orthorhombic space group. The electron density for, the N5-(2-nitrobutyl)-1,5-dihydro-FAD covalent intermediate is clearly, resolved. The structure of ES was used to solve the crystal structure of, oxidized NAO at 2.07 A resolution. The c axis for the trigonal space group, of oxidized NAO is 485 A, and there are six subunits (1(1)/(2), holoenzymes) in the asymmetric unit. Four of the active sites contain, spermine (EI), a weak competitive inhibitor, and two do not contain, spermine (E(ox)). The active-site structures of E(ox), EI, and ES* reveal, a hydrophobic channel that extends from the exterior of the protein and, terminates at Asp402 and the N5 position on the re face of the FAD. Thus, Asp402 is in the correct position to serve as the active-site base, where, it is proposed to abstract the alpha proton from neutral nitroalkane, substrates. The structures for NAO and various members of the ACAD family, overlay with root-mean-square deviations between 1.7 and 3.1 A. The, homologous region typically spans more than 325 residues and includes, Glu376, which is the active-site base in the prototypical member of the, ACAD family. However, NAO and the ACADs exhibit differences in, hydrogen-bonding patterns between the respective active-site base, substrate molecules, and FAD. These likely differentiate NAO from the, homologues and, consequently, are proposed to result in the unique, reaction mechanism of NAO.
About this StructureAbout this Structure
2C12 is a Single protein structure of sequence from Fusarium oxysporum with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover., Nagpal A, Valley MP, Fitzpatrick PF, Orville AM, Biochemistry. 2006 Jan 31;45(4):1138-50. PMID:16430210
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