1cp6
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1cp6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cp6, resolution 1.9Å" /> '''1-BUTANEBORONIC ACID ...)
Next diff →
Revision as of 10:31, 20 November 2007
|
1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE
Overview
Hydrolases containing two metal ions connected by a bridging ligand, catalyze reactions important in carcinogensis, tissue repair, post-translational modification, control and regulation of biochemical, pathways, and protein degradation. The aminopeptidase from Aeromonas, proteolytica serves as a paradigm for the study of such bridged bimetallic, proteases since its three-dimensional structure is known to very high, resolution and its catalytic reaction is amenable to spectroscopic, examination. Herein, we report the X-ray crystal structure at 1.9 A, resolution of AAP complexed with 1-butaneboronic acid (BuBA). This, structure suggests that this complex represents a snapshot of the, proteolytic reaction in an arrested form between the Michaelis complex and, the transition state. Comparison of the structure with spectroscopic and, other data allows us to conclude that the apparently structurally, symmetrical dizinc site is actually asymmetric electrostatically.
About this Structure
1CP6 is a Single protein structure of sequence from Vibrio proteolyticus with ZN and BUB as ligands. Active as Bacterial leucyl aminopeptidase, with EC number 3.4.11.10 Full crystallographic information is available from OCA.
Reference
1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development., De Paola CC, Bennett B, Holz RC, Ringe D, Petsko GA, Biochemistry. 1999 Jul 13;38(28):9048-53. PMID:10413478
Page seeded by OCA on Tue Nov 20 12:38:34 2007
