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[[Image:1mpx.gif|left|200px]]


{{Structure
==ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE==
|PDB= 1mpx |SIZE=350|CAPTION= <scene name='initialview01'>1mpx</scene>, resolution 1.90&Aring;
<StructureSection load='1mpx' size='340' side='right'caption='[[1mpx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[1mpx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_citri Xanthomonas citri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MPX FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amino-acid_esterase Alpha-amino-acid esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.43 3.1.1.43]  
</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>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1mpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mpx OCA], [https://pdbe.org/1mpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mpx RCSB], [https://www.ebi.ac.uk/pdbsum/1mpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mpx ProSAT]</span></td></tr>
 
</table>
'''ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE'''
== Function ==
 
[https://www.uniprot.org/uniprot/Q6YBS3_XANCI Q6YBS3_XANCI]  
 
== Evolutionary Conservation ==
==Overview==
[[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/mp/1mpx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1mpx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
alpha-Amino acid ester hydrolases (AEHs) catalyze the hydrolysis and synthesis of esters and amides with an alpha-amino group. As such, they can synthesize beta-lactam antibiotics from acyl compounds and beta-lactam nuclei obtained from the hydrolysis of natural antibiotics. This article describes the gene sequence and the 1.9-A resolution crystal structure of the AEH from Xanthomonas citri. The enzyme consists of an alpha/beta-hydrolase fold domain, a helical cap domain, and a jellyroll beta-domain. Structural homology was observed to the Rhodococcus cocaine esterase, indicating that both enzymes belong to the same class of bacterial hydrolases. Docking of a beta-lactam antibiotic in the active site explains the substrate specificity, specifically the necessity of an alpha-amino group on the substrate, and explains the low specificity toward the beta-lactam nucleus.
alpha-Amino acid ester hydrolases (AEHs) catalyze the hydrolysis and synthesis of esters and amides with an alpha-amino group. As such, they can synthesize beta-lactam antibiotics from acyl compounds and beta-lactam nuclei obtained from the hydrolysis of natural antibiotics. This article describes the gene sequence and the 1.9-A resolution crystal structure of the AEH from Xanthomonas citri. The enzyme consists of an alpha/beta-hydrolase fold domain, a helical cap domain, and a jellyroll beta-domain. Structural homology was observed to the Rhodococcus cocaine esterase, indicating that both enzymes belong to the same class of bacterial hydrolases. Docking of a beta-lactam antibiotic in the active site explains the substrate specificity, specifically the necessity of an alpha-amino group on the substrate, and explains the low specificity toward the beta-lactam nucleus.


==About this Structure==
The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases.,Barends TR, Polderman-Tijmes JJ, Jekel PA, Hensgens CM, de Vries EJ, Janssen DB, Dijkstra BW J Biol Chem. 2003 Jun 20;278(25):23076-84. Epub 2003 Apr 8. PMID:12684501<ref>PMID:12684501</ref>
1MPX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_citri Xanthomonas citri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPX OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases., Barends TR, Polderman-Tijmes JJ, Jekel PA, Hensgens CM, de Vries EJ, Janssen DB, Dijkstra BW, J Biol Chem. 2003 Jun 20;278(25):23076-84. Epub 2003 Apr 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12684501 12684501]
</div>
[[Category: Alpha-amino-acid esterase]]
<div class="pdbe-citations 1mpx" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xanthomonas citri]]
[[Category: Xanthomonas citri]]
[[Category: Barends, T R.M.]]
[[Category: Barends TRM]]
[[Category: Dijkstra, B W.]]
[[Category: Dijkstra BW]]
[[Category: Hensgens, C M.H.]]
[[Category: Hensgens CMH]]
[[Category: Janssen, D B.]]
[[Category: Janssen DB]]
[[Category: Jekel, P A.]]
[[Category: Jekel PA]]
[[Category: Polderman-Tijmes, J J.]]
[[Category: Polderman-Tijmes JJ]]
[[Category: Vries, E J.de.]]
[[Category: De Vries EJ]]
[[Category: CA]]
[[Category: GOL]]
[[Category: alpha/beta hydrolase]]
[[Category: jellyroll]]
[[Category: selenomethionine]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:39 2008''
Retrieved from "https://proteopedia.org/1mpx"