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| - | [[Image:1ft7.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ft7| PDB=1ft7 | SCENE= }} | | {{STRUCTURE_1ft7| PDB=1ft7 | SCENE= }} |
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| - | '''AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID'''
| + | ===AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11401547}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11401547 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11401547}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Peptidase]] | | [[Category: Peptidase]] |
| | [[Category: Zinc]] | | [[Category: Zinc]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:44:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:54:46 2008'' |
Revision as of 00:54, 1 July 2008
Template:STRUCTURE 1ft7
AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID
Template:ABSTRACT PUBMED 11401547
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 Tue Jul 1 03:54:46 2008
