1ft7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ft7.jpg|left|200px]]<br /><applet load="1ft7" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ft7.jpg|left|200px]]
-
caption="1ft7, resolution 2.2&Aring;" />
+
 
-
'''AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID'''<br />
+
{{Structure
 +
|PDB= 1ft7 |SIZE=350|CAPTION= <scene name='initialview01'>1ft7</scene>, resolution 2.2&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=PLU:LEUCINE PHOSPHONIC ACID'>PLU</scene>
 +
|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]
 +
|GENE=
 +
}}
 +
 
 +
'''AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1FT7 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>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=PLU:'>PLU</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=1FT7 OCA].
+
1FT7 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=1FT7 OCA].
==Reference==
==Reference==
-
Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis., Stamper C, Bennett B, Edwards T, Holz RC, Ringe D, Petsko G, Biochemistry. 2001 Jun 19;40(24):7035-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11401547 11401547]
+
Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis., Stamper C, Bennett B, Edwards T, Holz RC, Ringe D, Petsko G, Biochemistry. 2001 Jun 19;40(24):7035-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11401547 11401547]
[[Category: Bacterial leucyl aminopeptidase]]
[[Category: Bacterial leucyl aminopeptidase]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 26: Line 35:
[[Category: zinc]]
[[Category: zinc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:25 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:13:44 2008''

Revision as of 09:13, 20 March 2008

Image:1ft7.jpg


PDB ID 1ft7

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: , and
Activity: Bacterial leucyl aminopeptidase, with EC number 3.4.11.10
Coordinates: save as pdb, mmCIF, xml



AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID


Overview

The nature of the interaction of the transition-state analogue inhibitor L-leucinephosphonic acid (LPA) with the leucine aminopeptidase from Aeromonas proteolytica (AAP) was investigated. LPA was shown to be a competitive inhibitor at pH 8.0 with a K(i) of 6.6 microM. Electronic absorption spectra, recorded at pH 7.5 of [CoCo(AAP)], [CoZn(AAP)], and [ZnCo(AAP)] upon addition of LPA suggest that LPA interacts with both metal ions in the dinuclear active site. EPR studies on the Co(II)-substituted forms of AAP revealed that the environments of the Co(II) ions in both [CoZn(AAP)] and [ZnCo(AAP)] become highly asymmetric and constrained upon the addition of LPA and clearly indicate that LPA interacts with both metal ions. The X-ray crystal structure of AAP complexed with LPA was determined at 2.1 A resolution. The X-ray crystallographic data indicate that LPA interacts with both metal centers in the dinuclear active site of AAP and a single oxygen atom bridge is absent. Thus, LPA binds to the dinuclear active site of AAP as an eta-1,2-mu-phosphonate with one ligand to the second metal ion provided by the N-terminal amine. A structural comparison of the binding of phosphonate-containing transition-state analogues to the mono- and bimetallic peptidases provides insight into the requirement for the second metal ion in bridged bimetallic peptidases. On the basis of the results obtained from the spectroscopic and X-ray crystallographic data presented herein along with previously reported mechanistic data for AAP, a new catalytic mechanism for the hydrolysis reaction catalyzed by AAP is proposed.

About this Structure

1FT7 is a Single protein structure of sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA.

Reference

Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis., Stamper C, Bennett B, Edwards T, Holz RC, Ringe D, Petsko G, Biochemistry. 2001 Jun 19;40(24):7035-46. PMID:11401547

Page seeded by OCA on Thu Mar 20 11:13:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ft7"
Personal tools