 |
PDBsum entry 1rtq
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
The high-Resolution structures of the neutral and the low ph crystals of aminopeptidase from aeromonas proteolytica.
|
 |
|
Authors
|
 |
W.Desmarais,
D.L.Bienvenue,
K.P.Bzymek,
G.A.Petsko,
D.Ringe,
R.C.Holz.
|
 |
|
Ref.
|
 |
J Biol Inorg Chem, 2006,
11,
398-408.
|
 |
|
PubMed id
|
 |
|
 |
|
|
 |
 |
|
Abstract
|
 |
|
The aminopeptidase from Aeromonas proteolytica (AAP) contains two zinc ions in
the active site and catalyzes the degradation of peptides. Herein we report the
crystal structures of AAP at 0.95-A resolution at neutral pH and at 1.24-A
resolution at low pH. The combination of these structures allowed the precise
modeling of atomic positions, the identification of the metal bridging oxygen
species, and insight into the physical properties of the metal ions. On the
basis of these structures, a new putative catalytic mechanism is proposed for
AAP that is likely relevant to all binuclear metalloproteases.
|
 |
|
|
|
|
 |