1cp6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:29, 30 October 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1cp6.jpg|left|200px]]
 
-
{{Structure
+
==1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE==
-
|PDB= 1cp6 |SIZE=350|CAPTION= <scene name='initialview01'>1cp6</scene>, resolution 1.9&Aring;
+
<StructureSection load='1cp6' size='340' side='right'caption='[[1cp6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=BUB:1-BUTANE BORONIC ACID'>BUB</scene>
+
<table><tr><td colspan='2'>[[1cp6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CP6 FirstGlance]. <br>
-
|ACTIVITY= [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]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BUB:1-BUTANE+BORONIC+ACID'>BUB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
}}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cp6 OCA], [https://pdbe.org/1cp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cp6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cp6 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/AMPX_VIBPR AMPX_VIBPR]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/1cp6_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cp6 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
'''1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE'''
+
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<ref>PMID:10413478</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1cp6" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
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.
+
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1CP6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CP6 OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/10413478 10413478]
+
-
[[Category: Bacterial leucyl aminopeptidase]]
+
-
[[Category: Single protein]]
+
[[Category: Vibrio proteolyticus]]
[[Category: Vibrio proteolyticus]]
-
[[Category: Bennett, B.]]
+
[[Category: Bennett B]]
-
[[Category: Depaola, C C.]]
+
[[Category: Depaola CC]]
-
[[Category: Holz, R C.]]
+
[[Category: Holz RC]]
-
[[Category: Petsko, G A.]]
+
[[Category: Petsko GA]]
-
[[Category: Ringe, D.]]
+
[[Category: Ringe D]]
-
[[Category: BUB]]
+
-
[[Category: ZN]]
+
-
[[Category: aminopeptidase]]
+
-
[[Category: hydrolase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:27:10 2008''
+

Current revision

1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE

PDB ID 1cp6

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools