PDBsum entry 1jvb

Oxidoreductase

PDB id: 1jvb

Contents

Protein chain

347 a.a. *

Metals

_ZN ×2

Waters ×193

* Residue conservation analysis

PDB id:

1jvb

Name:

Oxidoreductase

Title:

Alcohol dehydrogenase from the archaeon sulfolobus solfataricus

Structure:

NAD(h)-dependent alcohol dehydrogenase. Chain: a. Fragment: apo-enzyme form. Engineered: yes. Other_details: apo-enzyme form

Source:

Sulfolobus solfataricus. Organism_taxid: 2287. Gene: adh. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PDB file)

Resolution:

1.85Å R-factor: 0.191 R-free: 0.220

Authors:

L.Esposito,F.Sica,A.Zagari,L.Mazzarella

Key ref:

L.Esposito et al. (2002). Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 A resolution. J Mol Biol, 318, 463-477. PubMed id: 12051852 DOI: 10.1016/S0022-2836(02)00088-8

Date:

29-Aug-01 Release date: 29-Aug-02

Protein chain

P39462  (ADH_SULSO) -  NAD-dependent alcohol dehydrogenase from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Seq: 347 a.a.

Struc: 347 a.a.

Enzyme reactions

• Enzyme class: E.C.1.1.1.1 - alcohol dehydrogenase.
• Reaction:
  1. a primary alcohol + NAD⁺ = an aldehyde + NADH + H⁺
  2. a secondary alcohol + NAD⁺ = a ketone + NADH + H⁺
• Cofactor: Zn(2+) or Fe cation

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/S0022-2836(02)00088-8

J Mol Biol 318:463-477 (2002)

PubMed id: 12051852

Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 A resolution.

L.Esposito, F.Sica, C.A.Raia, A.Giordano, M.Rossi, L.Mazzarella, A.Zagari.

ABSTRACT

The crystal structure of a medium-chain NAD(H)-dependent alcohol dehydrogenase (ADH) from an archaeon has been solved by multiwavelength anomalous diffraction, using a selenomethionine-substituted enzyme. The protein (SsADH), extracted from the hyperthermophilic organism Sulfolobus solfataricus, is a homo-tetramer with a crystallographic 222 symmetry. Despite the low level of sequence identity, the overall fold of the monomer is similar to that of the other homologous ADHs of known structure. However, a significant difference is the orientation of the catalytic domain relative to the coenzyme-binding domain that results in a larger interdomain cleft. At the bottom of this cleft, the catalytic zinc ion is coordinated tetrahedrally and lacks the zinc-bound water molecule that is usually found in ADH apoform structures. The fourth coordination position is indeed occupied by a Glu residue, as found in bacterial tetrameric ADHs. Other differences are found in the architecture of the substrate pocket whose entrance is more restricted than in other ADHs. SsADH is the first tetrameric ADH X-ray structure containing a second zinc ion playing a structural role. This latter metal ion shows a peculiar coordination, with a glutamic acid residue replacing one of the four cysteine ligands that are highly conserved throughout the structural zinc-containing dimeric ADHs.

Selected figure(s)

Figure 1.
Figure 1. A stereo view of the SsADH subunit. The C^a trace is marked with a ball every tenth C^a atom. Figure 1, Figure 3 and Figure 4 were prepared with MOLSCRIPT. [48.]

Figure 5.
Figure 5. Ribbon diagram of the SsADH homo-tetramer generated from crystallographic symmetry. The tetramer is a dimer of dimers (A/B and C/D). The catalytic zinc ions are coloured green. The Figure was prepared with MOLSCRIPT[48.] and Raster3D. [50.]

The above figures are reprinted by permission from Elsevier: J Mol Biol (2002, 318, 463-477) copyright 2002.

Figures were selected by an automated process.