 |
PDBsum entry 1d3a
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
1d3a
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 a resolution structures of the wild type and a mutant of malate dehydrogenase from haloarcula marismortui.
|
|
|
Authors
|
|
S.B.Richard,
D.Madern,
E.Garcin,
G.Zaccai.
|
|
|
Ref.
|
|
Biochemistry, 2000,
39,
992.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Previous biophysical studies of tetrameric malate dehydrogenase from the
halophilic archaeon Haloarcula marismortui (Hm MalDH) have revealed the
importance of protein-solvent interactions for its adaptation to molar salt
conditions that strongly affect protein solubility, stability, and activity, in
general. The structures of the E267R stability mutant of apo (-NADH) Hm MalDH
determined to 2.6 A resolution and of apo (-NADH) wild type Hm MalDH determined
to 2.9 A resolution, presented here, highlight a variety of novel
protein-solvent features involved in halophilic adaptation. The tetramer appears
to be stabilized by ordered water molecule networks and intersubunit complex
salt bridges "locked" in by bound solvent chloride and sodium ions. The E267R
mutation points into a central ordered water cavity, disrupting protein-solvent
interactions. The analysis of the crystal structures showed that halophilic
adaptation is not aimed uniquely at "protecting" the enzyme from the extreme
salt conditions, as may have been expected, but, on the contrary, consists of
mechanisms that harness the high ionic concentration in the environment.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Protocol 21: the mpd-Nacl-H2o system for the crystallization of halophilic proteins
|
|
|
Authors
|
|
S.B.Richard,
F.Bonnete,
O.Dym,
G.Zaccai.
|
|
|
Ref.
|
|
archaea : a laboratory 149 1995 manual ...
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Structural features stabilizing halophilic malate dehydrogenase from an archaebacterium
|
|
|
Authors
|
|
O.Dym,
M.Mevarech,
J.L.Sussman.
|
|
|
Ref.
|
|
science, 1995,
267,
1344.
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
Mutation at a single amino acid enhances the halophilic behaviour of malate dehydrogenase from haloarcula marismortui in physiological salts
|
|
|
Authors
|
|
D.Madern,
C.Pfister,
G.Zaccai.
|
|
|
Ref.
|
|
eur j biochem, 1995,
230,
1088.
|
|
|
|
Secondary reference #4
|
|
|
Title
|
|
Cloning, Sequencing, And expression in escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium haloarcula marismortui.
|
|
|
Authors
|
|
F.Cendrin,
J.Chroboczek,
G.Zaccai,
H.Eisenberg,
M.Mevarech.
|
|
|
Ref.
|
|
Biochemistry, 1993,
32,
4308-4313.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
