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1ft7

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[[Image:1ft7.jpg|left|200px]]
 
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{{Structure
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==AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID==
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|PDB= 1ft7 |SIZE=350|CAPTION= <scene name='initialview01'>1ft7</scene>, resolution 2.2&Aring;
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<StructureSection load='1ft7' size='340' side='right'caption='[[1ft7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|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>
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<table><tr><td colspan='2'>[[1ft7]] 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=1FT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FT7 FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ft7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ft7 OCA], [https://pdbe.org/1ft7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ft7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ft7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ft7 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1amp|1AMP]], [[1cp6|1CP6]]
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</table>
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|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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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AMPX_VIBPR AMPX_VIBPR]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/1ft7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ft7 ConSurf].
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<div style="clear:both"></div>
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'''AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID'''
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==See Also==
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Bacterial leucyl aminopeptidase]]
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[[Category: Single protein]]
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[[Category: Vibrio proteolyticus]]
[[Category: Vibrio proteolyticus]]
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[[Category: Bennett, B.]]
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[[Category: Bennett B]]
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[[Category: Holz, R.]]
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[[Category: Holz R]]
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[[Category: Petsko, G.]]
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[[Category: Petsko G]]
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[[Category: Ringe, D.]]
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[[Category: Ringe D]]
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[[Category: Stamper, C.]]
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[[Category: Stamper C]]
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[[Category: bimetallic]]
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[[Category: peptidase]]
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[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:29:50 2008''
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Current revision

AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID

PDB ID 1ft7

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