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2d38
From Proteopedia
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|PDB= 2d38 |SIZE=350|CAPTION= <scene name='initialview01'>2d38</scene>, resolution 2.05Å | |PDB= 2d38 |SIZE=350|CAPTION= <scene name='initialview01'>2d38</scene>, resolution 2.05Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> | + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2d36|2D36]], [[2d37|2D37]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d38 OCA], [http://www.ebi.ac.uk/pdbsum/2d38 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d38 RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Okai, M.]] | [[Category: Okai, M.]] | ||
[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
| - | [[Category: FMN]] | ||
| - | [[Category: NAP]] | ||
[[Category: flavin reductase]] | [[Category: flavin reductase]] | ||
| - | ''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 02:29:43 2008'' |
Revision as of 23:29, 30 March 2008
| |||||||
| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 2D36, 2D37
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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