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1bpn

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DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY

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Retrieved from "http://52.214.119.220/wiki/index.php/1bpn"

Categories: Bos taurus | Large Structures | Kim H | Lipscomb WN

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-[[Image:1bpn.jpg|left|200px]]<br /><applet load="1bpn" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1bpn, resolution 2.9&Aring;" />
-'''DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY'''<br />
-==Overview==
+==DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY==
-The tightly binding and readily exchanging metal binding sites in the, active site of bovine lens leucine aminopeptidase (blLAP; EC 3.4.11.1), have been differentiated and identified by x-ray crystallography. In, native blLAP,Zn2+ occupies both binding sites. In solution, site 1 readily, exchanges Zn2+ for other divalent cations, including Mg2+. The Zn2+ in, site 2 is unavailable for metal exchange under conditions which allow, exchange at site 1. The Zn2+/Mg2+ metal hybrid of blLAP (Mg-blLAP) was, prepared in solution and crystallized. X-ray diffraction data to 2.9-A, resolution were collected at -150 degrees C from single crystals of, Mg-blLAP and native blLAP. Comparisons of omit maps calculated from the, Mg-blLAP data with analogous maps calculated from the native blLAP data, show electron density in one of the metal binding sites in Mg-blLAP which, is much weaker than the electron density in the other binding site. Since, there are fewer electrons associated with Mg2+ than with Zn2+, the, difference in electron density between the two metal binding sites is, consistent with occupancy of the weaker electron density site by Mg2+ and, identifies this metal binding site as site 1, defined as the readily, exchanging site. The present identification of the metal binding sites, reverses the previous presumptive assignment of the metal binding sites, which was based on the structure of native blLAP [Burley, S. K., David, P., R., Sweet, R. M., Taylor, A. &amp; Lipscomb, W. N. (1992) J. Mol. Biol. 224, 113-140]. According to the residue-numbering convention of native blLAP, the new assignment of the metal binding sites identifies the readily, exchanging site 1 with Zn-488, which is within interaction distance of one, side-chain carboxylate oxygen from each of Asp-255, Asp-332, and Glu-334, and the main-chain carbonyl oxygen of Asp-332. The more tightly binding, site 2 is identified with Zn-489, which is within interaction distance of, one side-chain carboxylate oxygen from each of Asp-255, Asp-273, and, Glu-334 and the side-chain amine nitrogen of Lys-250.
+<StructureSection load='1bpn' size='340' side='right'caption='[[1bpn]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1bpn]] 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=1BPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BPN FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
+<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bpn OCA], [https://pdbe.org/1bpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bpn RCSB], [https://www.ebi.ac.uk/pdbsum/1bpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bpn ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bp/1bpn_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1bpn ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-BPN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] 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=1BPN OCA].
+*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography., Kim H, Lipscomb WN, Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5006-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8506345 8506345]
+[[Category: Bos taurus]]
-[[Category: Leucyl aminopeptidase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Kim H]]
-[[Category: Kim, H.]]
+[[Category: Lipscomb WN]]
-[[Category: Lipscomb, W.N.]]
-[[Category: ZN]]
-[[Category: hydrolase(alpha-aminoacylpeptide)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:49:10 2007''

1bpn

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DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY

Structural highlights

Function

Evolutionary Conservation

See Also

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