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1lap

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(New page: 200px<br /><applet load="1lap" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lap, resolution 2.7&Aring;" /> '''MOLECULAR STRUCTURE O...)
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[[Image:1lap.jpg|left|200px]]<br /><applet load="1lap" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lap, resolution 2.7&Aring;" />
 
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'''MOLECULAR STRUCTURE OF LEUCINE AMINOPEPTIDASE AT 2.7-ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==MOLECULAR STRUCTURE OF LEUCINE AMINOPEPTIDASE AT 2.7-ANGSTROMS RESOLUTION==
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The three-dimensional structure of bovine lens leucine aminopeptidase (EC, 3.4.11.1) complexed with bestatin, a slow-binding inhibitor, has been, solved to 3.0-A resolution by the multiple isomorphous replacement method, with phase combination and density modification. In addition, the, structure of the isomorphous native enzyme has been refined at 2.7-A, resolution, and the current crystallographic R factor is 0.169 for a model, that includes the two zinc ions and all 487 amino acid residues comprising, the asymmetric unit. The enzyme is physiologically active as a hexamer, which has 32 symmetry and is triangular in shape with a triangle edge, length of 115 A and maximal thickness of 90 A. The monomers are, crystallographically equivalent and each is folded into two unequal, alpha/beta domains connected by an alpha-helix to give a comma-like shape, with approximate maximal dimensions of 90 x 55 x 55 A3. The secondary, structural composition is 40% alpha-helix and 19% beta-strand. The, N-terminal domain (160 amino acids) mediates trimer-trimer interactions, and does not appear to participate directly in catalysis. The C-terminal, domain (327 amino acids) is responsible for catalysis and binds the two, zinc ions, which are 2.88 A apart. The pair of metal ions is located near, the edge of an eight-stranded, saddle-shaped beta-sheet. One zinc ion is, coordinated by carboxylate oxygen atoms of Asp-255, Asp-332, and Glu-334, and the carbonyl oxygen of Asp-332. The other zinc ion is coordinated by, the carboxylate oxygen atoms of Asp-255, Asp-273, and Glu-334. The active, site also contains two positively charged residues, Lys-250 and Arg-336., The six active sites are themselves located in the interior of the, hexamer, where they line a disk-shaped cavity of radius 15 A and thickness, 10 A. Access to this cavity is provided by solvent channels that run along, the twofold symmetry axes.
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<StructureSection load='1lap' size='340' side='right'caption='[[1lap]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lap]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LAP FirstGlance]. <br>
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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]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=1lap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lap OCA], [https://pdbe.org/1lap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lap RCSB], [https://www.ebi.ac.uk/pdbsum/1lap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lap ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMPL_BOVIN AMPL_BOVIN] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
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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/la/1lap_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=1lap ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1LAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Leucyl_aminopeptidase Leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.1 3.4.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LAP OCA].
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Molecular structure of leucine aminopeptidase at 2.7-A resolution., Burley SK, David PR, Taylor A, Lipscomb WN, Proc Natl Acad Sci U S A. 1990 Sep;87(17):6878-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2395881 2395881]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Leucyl aminopeptidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Burley SK]]
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[[Category: Burley, S.K.]]
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[[Category: David PR]]
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[[Category: David, P.R.]]
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[[Category: Lipscomb WN]]
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[[Category: Lipscomb, W.N.]]
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[[Category: Taylor A]]
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[[Category: Taylor, A.]]
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[[Category: ZN]]
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[[Category: hydrolase(alpha-aminoacylpeptide)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:25:55 2007''
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Current revision

MOLECULAR STRUCTURE OF LEUCINE AMINOPEPTIDASE AT 2.7-ANGSTROMS RESOLUTION

PDB ID 1lap

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