PDBsum entry 1a27

Dehydrogenase

PDB id: 1a27

Contents

Protein chain

285 a.a.

Ligands

EST

NAP

Waters ×157

References listed in PDB file

Key reference

Title

Crystallization and X-Ray crystallographic analysis of recombinant chicken poly(ADP-Ribose) polymerase catalytic domain produced in sf9 insect cells.

Authors

S.Jung, E.A.Miranda, J.M.De murcia, C.Niedergang, M.Delarue, G.E.Schulz, G.M.De murcia.

Ref.

J Mol Biol, 1994, 244, 114-116.

PubMed id

7966315

Abstract

Poly (ADP-ribose) polymerase (PARP) participates in the immediate response in mammalian cells exposed to DNA-damaging agents. Recombinant baculovirus harboring the cDNA of the chicken PARP catalytic domain (40 kDa) have been used to infect Spodoptera frugiperda (Sf9) insect cells. The recombinant polypeptide (30 mg per 1 x 10(9) cells) was purified to homogeneity by 3-aminobenzamide affinity chromatography. The enzymatic properties of the recombinant domain were similar to those of the native fragment. Crystals of the purified recombinant catalytic domain were grown by vapor diffusion. The crystals belong to space group P2(1)2(1)2(1) with unit cell dimensions of a = 59.2 A, b = 65.0 A, c = 96.9 A. They are suitable for X-ray analysis and diffract to 2.0 A.

Secondary reference #1

Title

Unusual charge stabilization of NADP+ in 17beta-Hydroxysteroid dehydrogenase.

Authors

C.Mazza, R.Breton, D.Housset, J.C.Fontecilla-Camps.

Ref.

J Biol Chem, 1998, 273, 8145-8152. [DOI no: 10.1074/jbc.273.14.8145]

PubMed id

9525918

Figure 3.
Fig. 3. Superposition of the 187-209 loop of the wild-type 17 -HSD1 model (1bhs (24)) (medium gray) and the monomer mC of the H221L·E2·NAD^+ complex (black) with the 182-203 loop of the MLCR model (1cyd (22)) (light gray). Phe^192 of the H221L mutant and Met186 of MLCR superpose very well and make extensive hydrophobic contacts with the nicotinamide ring. Lys195 of the H221L model interacts with the 2'-phosphate while no equivalent residue is found for MLCR.

Figure 6.
Fig. 6. Stereoscopic view of the steroid binding site of wild-type (1fdt model in yellow, and 1fds model in orange), H221L (monomers mC in blue, mD in light blue), and H221Q (pink). Phe^226 of the 1fdt model and Gln221 of the H221Q mutant are shown with their two modeled conformations. The steroid environment is very well conserved, especially Phe^155 and Ser142 which are the residues involved in the catalytic reaction. Significant deviations are observed for the steroid, especially for its C and D rings.

The above figures are reproduced from the cited reference with permission from the ASBMB

Secondary reference #2

Title

The structure of a complex of human 17beta-Hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors.

Authors

R.Breton, D.Housset, C.Mazza, J.C.Fontecilla-Camps.

Ref.

Structure, 1996, 4, 905-915. [DOI no: 10.1016/S0969-2126(96)00098-6]

PubMed id

8805577

Figure 3.
Figure 3. Stereoscopic view of the residues of 17β-HSD1 (light grey) interacting with the estradiol molecule (dark grey). Phe226 is shown with its two modelled conformations. Figure 3. Stereoscopic view of the residues of 17β-HSD1 (light grey) interacting with the estradiol molecule (dark grey). Phe226 is shown with its two modelled conformations.

Figure 6.
Figure 6. Scheme of interactions between NADP^+ and 17β-HSD1, at −150°C. Dashed lines represent hydrogen bonds. Figure 6. Scheme of interactions between NADP^+ and 17β-HSD1, at −150°C. Dashed lines represent hydrogen bonds.

The above figures are reproduced from the cited reference with permission from Cell Press

Secondary reference #3

Title

Structure of human estrogenic 17 beta-Hydroxysteroid dehydrogenase at 2.20 a resolution.

Authors

D.Ghosh, V.Z.Pletnev, D.W.Zhu, Z.Wawrzak, W.L.Duax, W.Pangborn, F.Labrie, S.X.Lin.

Ref.

Structure, 1995, 3, 503-513. [DOI no: 10.1016/S0969-2126(01)00183-6]

PubMed id

7663947

Figure 1.
Figure 1. (a) Stereo ribbon diagram of a monomer of human estrogenic 17β-hydroxysteroid dehydrogenase (HSD). The course of the polypeptide chain is shown for residues 1–284. α-helices are drawn as magenta coils, β-strands as blue arrows, and turns and loops as green ropes. The side chains for residues in the active site belonging to the catalytic triad, Tyr155-Lys159-Ser142, are shown in white. The view is almost parallel to the central β-sheet. (Figure prepared using the program SETOR [43].) (b) Folding topology of strands (triangles) and helices (circles) in 17β-HSD. Figure 1. (a) Stereo ribbon diagram of a monomer of human estrogenic 17β-hydroxysteroid dehydrogenase (HSD). The course of the polypeptide chain is shown for residues 1–284. α-helices are drawn as magenta coils, β-strands as blue arrows, and turns and loops as green ropes. The side chains for residues in the active site belonging to the catalytic triad, Tyr155-Lys159-Ser142, are shown in white. The view is almost parallel to the central β-sheet. (Figure prepared using the program SETOR [[4]43].) (b) Folding topology of strands (triangles) and helices (circles) in 17β-HSD.

Figure 9.
Figure 9. Helices (a) αG′ and (b) αH viewed along the helical axis. The side chains are color coded to illustrate their amphiphilicity, as follows: green, hydrophobic; red, charged; and magenta, residues having a proton-donating functional group. Figure 9. Helices (a) αG′ and (b) αH viewed along the helical axis. The side chains are color coded to illustrate their amphiphilicity, as follows: green, hydrophobic; red, charged; and magenta, residues having a proton-donating functional group. (Figure prepared using the program SETOR [[3]43].)

The above figures are reproduced from the cited reference with permission from Cell Press