1cp6: Difference between revisions

Revision as of 13:08, 21 February 2008

1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE

OverviewOverview

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 StructureAbout this Structure

1CP6 is a Single protein structure of sequence from Vibrio proteolyticus with and as ligands. Active as Bacterial leucyl aminopeptidase, with EC number 3.4.11.10 Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 12:08:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1cp6.jpg|left|200px]]<br /><applet load="1cp6" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cp6.jpg|left|200px]]<br /><applet load="1cp6" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cp6, resolution 1.9&Aring;" />
 '''1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE'''<br />
 ==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.
+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==
-CP6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus] with ZN and BUB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CP6 OCA].
+CP6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=BUB:'>BUB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CP6 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Vibrio proteolyticus]]
 [[Category: Bennett, B.]]
-[[Category: Depaola, C.C.]]
+[[Category: Depaola, C C.]]
-[[Category: Holz, R.C.]]
+[[Category: Holz, R C.]]
-[[Category: Petsko, G.A.]]
+[[Category: Petsko, G A.]]
 [[Category: Ringe, D.]]
 [[Category: BUB]]
@@ Line 24: / Line 24: @@
 [[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:38:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:17 2008''