1ft7
From Proteopedia
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|PDB= 1ft7 |SIZE=350|CAPTION= <scene name='initialview01'>1ft7</scene>, resolution 2.2Å | |PDB= 1ft7 |SIZE=350|CAPTION= <scene name='initialview01'>1ft7</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PLU:LEUCINE+PHOSPHONIC+ACID'>PLU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1amp|1AMP]], [[1cp6|1CP6]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ft7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ft7 OCA], [http://www.ebi.ac.uk/pdbsum/1ft7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ft7 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: Stamper, C.]] | [[Category: Stamper, C.]] | ||
| - | [[Category: K]] | ||
| - | [[Category: PLU]] | ||
| - | [[Category: ZN]] | ||
[[Category: bimetallic]] | [[Category: bimetallic]] | ||
[[Category: peptidase]] | [[Category: peptidase]] | ||
[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:29:50 2008'' |
Revision as of 17:29, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Bacterial leucyl aminopeptidase, with EC number 3.4.11.10 | ||||||
| Related: | 1AMP, 1CP6
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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