This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.




1lan

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1lan" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lan, resolution 1.9&Aring;" /> '''LEUCINE AMINOPEPTIDAS...)
Current revision (07:31, 14 February 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lan.gif|left|200px]]<br /><applet load="1lan" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1lan, resolution 1.9&Aring;" />
 
-
'''LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL'''<br />
 
-
==Overview==
+
==LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL==
-
The three-dimensional structures of bovine lens leucine aminopeptidase, (blLAP) complexed with L-leucinal and of the unliganded enzyme have been, determined at crystallographic resolutions of 1.9 and 1.6 A, respectively., Leucinal binds as a hydrated gem-diol to the active site of b1LAP), resembling the presumed gem-diolated intermediate in the catalytic, pathway. One hydroxyl group bridges the two active site metal ions, and, the other OH group is coordinated to Zn1. The high-resolution structure of, the unliganded enzyme reveals one metal-bound water ligand, which is, bridging both zinc ions. Together, these structures support a mechanism in, which the bridging water ligand is the attacking hydroxide ion, nucleophile. The gem-diolate intermediate is probably stabilized by four, coordinating bonds to the dizinc center and by interaction with Lys-262, and Arg-336. In the mechanism, Lys-262 polarizes the peptide carbonyl, group, which is also coordinated to Zn1. The Arg-336 side chain interacts, with the substrate and the gem-diolate intermediate via water molecules., Near Arg-336 in the b1LAP-leucinal structure, an unusually short hydrogen, bond is found between two active site water molecules.
+
<StructureSection load='1lan' size='340' side='right'caption='[[1lan]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1lan]] 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=1LAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LAN 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]] 1.9&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <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=1lan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lan OCA], [https://pdbe.org/1lan PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lan RCSB], [https://www.ebi.ac.uk/pdbsum/1lan PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lan 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/la/1lan_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=1lan ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1LAN 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, LEU 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=1LAN OCA].
+
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography., Strater N, Lipscomb WN, Biochemistry. 1995 Nov 14;34(45):14792-800. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7578088 7578088]
+
[[Category: Bos taurus]]
[[Category: Bos taurus]]
-
[[Category: Leucyl aminopeptidase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Lipscomb WN]]
-
[[Category: Lipscomb, W.N.]]
+
[[Category: Straeter N]]
-
[[Category: Straeter, N.]]
+
-
[[Category: LEU]]
+
-
[[Category: MRD]]
+
-
[[Category: ZN]]
+
-
[[Category: aminopeptidase]]
+
-
[[Category: exopeptidase]]
+
-
[[Category: metallopeptidase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:25:50 2007''
+

Current revision

LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL

PDB ID 1lan

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lan"
Personal tools