2ek8

<StructureSection load='2ek8' size='340' side='right' caption='[[2ek8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[2ek8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aneurinibacillus_sp._am-1 Aneurinibacillus sp. am-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EK8 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ek9|2ek9]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ek8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ek8 OCA], [http://pdbe.org/2ek8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ek8 RCSB], [http://www.ebi.ac.uk/pdbsum/2ek8 PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ek/2ek8_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

To elucidate the structure and molecular mechanism of a characteristic proline-specific aminopeptidase produced by the thermophile Aneurinibacillus sp. strain AM-1, its gene was cloned and the recombinant protein was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 1.8 A resolution from the recombinant aminopeptidase crystal. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 93.62, b = 68.20, c = 76.84 A. A complete data set was also obtained from crystals of SeMet-substituted aminopeptidase. Data in the resolution range 20-2.1 A from the MAD data set from the SeMet-substituted crystal were used for phase determination.

Overexpression, purification, crystallization and preliminary X-ray crystallographic studies of a proline-specific aminopeptidase from Aneurinibacillus sp. strain AM-1.,Akioka M, Nakano H, Horikiri A, Tsujimoto Y, Matsui H, Shimizu T, Nakatsu T, Kato H, Watanabe K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1266-8. Epub 2006 Nov 30. PMID:17142913<ref>PMID:17142913</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2ek8" style="background-color:#fffaf0;"></div>

*[[Aminopeptidase|Aminopeptidase]]

[[Category: Aneurinibacillus sp. am-1]]

[[Category: Akioka, M]]

[[Category: Nakano, H]]

[[Category: Watanabe, K]]

[[Category: Hydrolase]]

[[Category: Metalloproteinase]]