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[[Image:1kec.png|left|200px]]


{{STRUCTURE_1kec| PDB=1kec | SCENE= }}
==PENICILLIN ACYLASE MUTANT WITH PHENYL PROPRIONIC ACID==
<StructureSection load='1kec' size='340' side='right'caption='[[1kec]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KEC 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]] 2.3&#8491;</td></tr>
<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=GRO:R-2-PHENYL-PROPRIONIC+ACID'>GRO</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=1kec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kec OCA], [https://pdbe.org/1kec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kec RCSB], [https://www.ebi.ac.uk/pdbsum/1kec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kec ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAC_ECOLX PAC_ECOLX]
== 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/ke/1kec_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=1kec ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Penicillin acylase catalyses the condensation of Calpha-substituted phenylacetic acids with beta-lactam nucleophiles, producing semi-synthetic beta-lactam antibiotics. For efficient synthesis a low affinity for phenylacetic acid and a high affinity for Calpha-substituted phenylacetic acid derivatives is desirable. We made three active site mutants, alphaF146Y, betaF24A and alphaF146Y/betaF24A, which all had a 2- to 10-fold higher affinity for Calpha-substituted compounds than wild-type enzyme. In addition, betaF24A had a 20-fold reduced affinity for phenylacetic acid. The molecular basis of the improved properties was investigated by X-ray crystallography. These studies showed that the higher affinity of alphaF146Y for (R)-alpha-methylphenylacetic acid can be explained by van der Waals interactions between alphaY146:OH and the Calpha-substituent. The betaF24A mutation causes an opening of the phenylacetic acid binding site. Only (R)-alpha-methylphenylacetic acid, but not phenylacetic acid, induces a conformation with the ligand tightly bound, explaining the weak binding of phenylacetic acid. A comparison of the betaF24A structure with other open conformations of penicillin acylase showed that betaF24 has a fixed position, whereas alphaF146 acts as a flexible lid on the binding site and reorients its position to achieve optimal substrate binding.


===PENICILLIN ACYLASE MUTANT WITH PHENYL PROPRIONIC ACID===
Structural and kinetic studies on ligand binding in wild-type and active-site mutants of penicillin acylase.,Alkema WB, Hensgens CM, Snijder HJ, Keizer E, Dijkstra BW, Janssen DB Protein Eng Des Sel. 2004 May;17(5):473-80. Epub 2004 Jul 14. PMID:15254299<ref>PMID:15254299</ref>


{{ABSTRACT_PUBMED_15254299}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kec" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
[[1kec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEC OCA].
*[[Penicillin acylase|Penicillin acylase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:015254299</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Penicillin amidase]]
[[Category: Large Structures]]
[[Category: Dijkstra, B W.]]
[[Category: Dijkstra BW]]
[[Category: Hensgens, C M.H.]]
[[Category: Hensgens CMH]]
[[Category: Keizer, E.]]
[[Category: Keizer E]]
[[Category: Snijder, H J.]]
[[Category: Snijder HJ]]
[[Category: Beta-strand]]
[[Category: Helice]]
[[Category: Hydrolase]]
[[Category: Ntn-hydrolase fold]]
[[Category: Phenyl proprionic acid]]

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