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2d38

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(New page: 200px<br /><applet load="2d38" size="350" color="white" frame="true" align="right" spinBox="true" caption="2d38, resolution 2.05&Aring;" /> '''The Crystal Structur...)
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==Overview==
==Overview==
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4-Hydroxyphenylacetate (4-HPA) is oxidized as an energy source by two, component enzymes, the large component (HpaB) and the small component, (HpaC). HpaB is a 4-HPA monooxygenase that utilizes FADH(2) supplied by a, flavin reductase HpaC. We determined the crystal structure of HpaC, (ST0723) from the aerobic thermoacidophilic crenarchaeon Sulfolobus, tokodaii strain 7 in its three states [NAD(P)(+)-free, NAD(+)-bound, and, NADP(+)-bound]. HpaC exists as a homodimer, and each monomer was found to, contain an FMN. HpaC preferred FMN to FAD because there was not enough, space to accommodate the AMP moiety of FAD in its flavin-binding site. The, most striking difference between the NAD(P)(+)-free and the, NAD(+)/NADP(+)-bound structures was observed in the N-terminal helix. The, N-terminal helices in the NAD(+)/NADP(+)-bound structures rotated ca. 20, degrees relative to the NAD(P)(+)-free structure. The bound NAD(+) has a, compact folded conformation with nearly parallel stacking rings of, nicotinamide and adenine. The nicotinamide of NAD(+) stacked the, isoalloxazine ring of FMN so that NADH could directly transfer hydride., The bound NADP(+) also had a compact conformation but was bound in a, reverse direction, which was not suitable for hydride transfer.
+
4-Hydroxyphenylacetate (4-HPA) is oxidized as an energy source by two component enzymes, the large component (HpaB) and the small component (HpaC). HpaB is a 4-HPA monooxygenase that utilizes FADH(2) supplied by a flavin reductase HpaC. We determined the crystal structure of HpaC (ST0723) from the aerobic thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7 in its three states [NAD(P)(+)-free, NAD(+)-bound, and NADP(+)-bound]. HpaC exists as a homodimer, and each monomer was found to contain an FMN. HpaC preferred FMN to FAD because there was not enough space to accommodate the AMP moiety of FAD in its flavin-binding site. The most striking difference between the NAD(P)(+)-free and the NAD(+)/NADP(+)-bound structures was observed in the N-terminal helix. The N-terminal helices in the NAD(+)/NADP(+)-bound structures rotated ca. 20 degrees relative to the NAD(P)(+)-free structure. The bound NAD(+) has a compact folded conformation with nearly parallel stacking rings of nicotinamide and adenine. The nicotinamide of NAD(+) stacked the isoalloxazine ring of FMN so that NADH could directly transfer hydride. The bound NADP(+) also had a compact conformation but was bound in a reverse direction, which was not suitable for hydride transfer.
==About this Structure==
==About this Structure==
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[[Category: Kamo, M.]]
[[Category: Kamo, M.]]
[[Category: Kudo, N.]]
[[Category: Kudo, N.]]
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[[Category: Lee, W.C.]]
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[[Category: Lee, W C.]]
[[Category: Nagata, K.]]
[[Category: Nagata, K.]]
[[Category: Okai, M.]]
[[Category: Okai, M.]]
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[[Category: flavin reductase]]
[[Category: flavin reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:54:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:56 2008''

Revision as of 14:54, 21 February 2008

Image:2d38.gif

2d38, resolution 2.05Å

Drag the structure with the mouse to rotate

The Crystal Structure of Flavin Reductase HpaC complexed with NADP+

Overview

4-Hydroxyphenylacetate (4-HPA) is oxidized as an energy source by two component enzymes, the large component (HpaB) and the small component (HpaC). HpaB is a 4-HPA monooxygenase that utilizes FADH(2) supplied by a flavin reductase HpaC. We determined the crystal structure of HpaC (ST0723) from the aerobic thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7 in its three states [NAD(P)(+)-free, NAD(+)-bound, and NADP(+)-bound]. HpaC exists as a homodimer, and each monomer was found to contain an FMN. HpaC preferred FMN to FAD because there was not enough space to accommodate the AMP moiety of FAD in its flavin-binding site. The most striking difference between the NAD(P)(+)-free and the NAD(+)/NADP(+)-bound structures was observed in the N-terminal helix. The N-terminal helices in the NAD(+)/NADP(+)-bound structures rotated ca. 20 degrees relative to the NAD(P)(+)-free structure. The bound NAD(+) has a compact folded conformation with nearly parallel stacking rings of nicotinamide and adenine. The nicotinamide of NAD(+) stacked the isoalloxazine ring of FMN so that NADH could directly transfer hydride. The bound NADP(+) also had a compact conformation but was bound in a reverse direction, which was not suitable for hydride transfer.

About this Structure

2D38 is a Single protein structure of sequence from Sulfolobus tokodaii str. 7 with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of the short-chain flavin reductase HpaC from Sulfolobus tokodaii strain 7 in its three states: NAD(P)(+)(-)free, NAD(+)(-)bound, and NADP(+)(-)bound., Okai M, Kudo N, Lee WC, Kamo M, Nagata K, Tanokura M, Biochemistry. 2006 Apr 25;45(16):5103-10. PMID:16618099

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