1lcp

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(New page: 200px<br /><applet load="1lcp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lcp, resolution 1.65&Aring;" /> '''BOVINE LENS LEUCINE ...)
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[[Image:1lcp.gif|left|200px]]<br /><applet load="1lcp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lcp, resolution 1.65&Aring;" />
 
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'''BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH L-LEUCINE PHOSPHONIC ACID'''<br />
 
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==Overview==
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==BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH L-LEUCINE PHOSPHONIC ACID==
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The three-dimensional structure of bovine lens leucine aminopeptidase, (blLAP) complexed with L-Leucinephosphonic acid (LeuP) has been determined, by molecular replacement using the structure of native blLAP as a starting, model. Cocrystallization of the enzyme with the inhibitor yielded a new, crystal form of space group P321 which has cell dimensions a = 130.4 A and, c = 125.4 A. Refinement of the model against data from 7.0 to 1.65 A, resolution resulted in a final structure with a crystallographic residual, of 0.160 (R(free) = 0.191). The N-terminal amino group of LeuP is, coordinated to Zn-489, one phosphoryl oxygen atom bridges both metal ions, and another phosphoryl oxygen atom is coordinated to Zn-488. The side, chain of Arg-336 interacts with the inhibitor via three water molecules., LeuP resembles the presumed tetrahedral gem-diolate transition state after, direct attack of a water or hydroxide ion nucleophile on the scissile, peptide bond. On the basis of the LeuP binding mode and the previous, structural and biochemical data, three plausible reaction pathways are, evaluated. The two-metal ion mechanisms discussed herein share as common, features a metal-bound hydroxide ion nucleophile and polarization of the, carbonyl group by the zinc ions. Possible catalytic roles of Arg-336 and, Lys-262 in the direct or indirect (through H2O) protonation of the leaving, group, in the stabilization of a zinc-bound OH- nucleophile and in the, stabilization of the negatively charged intermediate, are discussed. A, site 3 metal ion approximately 12 A away from the active site 2 zinc ion, probably serves a structural role.
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<StructureSection load='1lcp' size='340' side='right'caption='[[1lcp]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lcp]] is a 2 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=1LCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LCP 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]] 1.65&#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=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PLU:LEUCINE+PHOSPHONIC+ACID'>PLU</scene>, <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=1lcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lcp OCA], [https://pdbe.org/1lcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lcp RCSB], [https://www.ebi.ac.uk/pdbsum/1lcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lcp 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/lc/1lcp_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=1lcp 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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1LCP 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, PLU and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1LCP 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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Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 A resolution in a new crystal form., Strater N, Lipscomb WN, Biochemistry. 1995 Jul 18;34(28):9200-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7619821 7619821]
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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: Lipscomb WN]]
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[[Category: Lipscomb, W.N.]]
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[[Category: Straeter N]]
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[[Category: Straeter, N.]]
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[[Category: MRD]]
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[[Category: PLU]]
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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 20:28:54 2007''
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Current revision

BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH L-LEUCINE PHOSPHONIC ACID

PDB ID 1lcp

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