 |
PDBsum entry 1rhc
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
1rhc
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Coenzyme binding in f420-Dependent secondary alcohol dehydrogenase, A member of the bacterial luciferase family.
|
|
|
Authors
|
|
S.W.Aufhammer,
E.Warkentin,
H.Berk,
S.Shima,
R.K.Thauer,
U.Ermler.
|
|
|
Ref.
|
|
Structure, 2004,
12,
361-370.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
F(420)-dependent secondary alcohol dehydrogenase (Adf) from methanogenic archaea
is a member of the growing bacterial luciferase family which are all TIM barrel
enzymes, most of which with an unusual nonprolyl cis peptide bond. We report
here on the crystal structure of Adf from Methanoculleus thermophilicus at 1.8 A
resolution in complex with a F(420)-acetone adduct. The knowledge of the F(420)
binding mode in Adf provides the molecular basis for modeling F(420) and FMN
into the other enzymes of the family. A nonprolyl cis peptide bond was
identified as an essential part of a bulge that serves as backstop at the
Re-face of F(420) to keep it in a bent conformation. The acetone moiety of the
F(420)-acetone adduct is positioned at the Si-face of F(420) deeply buried
inside the protein. Isopropanol can be reliably modeled and a hydrogen transfer
mechanism postulated. His39 and Glu108 can be identified as key players for
binding of the acetone or isopropanol oxygens and for catalysis.
|
|
|
|
|
|
Figure 4.
Figure 4. The Nonprolyl cis Peptide Bond in AdfThe
nonprolyl cis peptide bond between Cys72 and Ile73 is an
essential constituent of a bulge that is directed toward the
F[420] binding site, causing a bent conformation of the
deazaisoalloxazine ring. The well-conserved Asp38, which would
partly interfere with a straight course of strand b3, is
strongly linked to the polypeptide chain and stabilizes the
bulge. These favorable interactions might compensate for the
energy lost when forming the nonprolyl cis peptide bond.
|
|
|
|
|
|
The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
361-370)
copyright 2004.
|
|
|
|
|
|
|
