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==Aminopeptidase from Aneurinibacillus sp. strain AM-1 with Bestatin==
==Aminopeptidase from Aneurinibacillus sp. strain AM-1 with Bestatin==
<StructureSection load='2ek9' size='340' side='right' caption='[[2ek9]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='2ek9' size='340' side='right'caption='[[2ek9]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ek9]] 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=2EK9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EK9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ek9]] is a 1 chain structure with sequence from [https://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=2EK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EK9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BES:2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC+ACID'>BES</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97&#8491;</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=2ek9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ek9 OCA], [http://pdbe.org/2ek9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ek9 RCSB], [http://www.ebi.ac.uk/pdbsum/2ek9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ek9 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BES:2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC+ACID'>BES</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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=2ek9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ek9 OCA], [https://pdbe.org/2ek9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ek9 RCSB], [https://www.ebi.ac.uk/pdbsum/2ek9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ek9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2V759_9BACL A2V759_9BACL]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2ek9 ConSurf].
</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=2ek9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<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>
</div>
<div class="pdbe-citations 2ek9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Aminopeptidase|Aminopeptidase]]
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aneurinibacillus sp. am-1]]
[[Category: Aneurinibacillus sp. AM-1]]
[[Category: Akioka, M]]
[[Category: Large Structures]]
[[Category: Nakano, H]]
[[Category: Akioka M]]
[[Category: Watanabe, K]]
[[Category: Nakano H]]
[[Category: Hydrolase]]
[[Category: Watanabe K]]
[[Category: Metalloproteinase]]

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