1k5q: Difference between revisions

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[[Image:1k5q.jpg|left|200px]]


{{Structure
==PENICILLIN ACYLASE, MUTANT COMPLEXED WITH PAA==
|PDB= 1k5q |SIZE=350|CAPTION= <scene name='initialview01'>1k5q</scene>, resolution 2.34&Aring;
<StructureSection load='1k5q' size='340' side='right'caption='[[1k5q]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PAC:2-PHENYLACETIC+ACID'>PAC</scene>
<table><tr><td colspan='2'>[[1k5q]] 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=1K5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K5Q FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34&#8491;</td></tr>
|GENE= PAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<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=PAC:2-PHENYLACETIC+ACID'>PAC</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k5q OCA], [https://pdbe.org/1k5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k5q RCSB], [https://www.ebi.ac.uk/pdbsum/1k5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k5q ProSAT]</span></td></tr>
|RELATEDENTRY=[[1pnk|1pnk]], [[1pnl|1pnl]], [[1fxv|1fxv]], [[1jx9|1JX9]], [[1ai4|1AI4]], [[1ai5|1AI5]], [[1ai6|1AI6]], [[1ai7|1AI7]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k5q OCA], [http://www.ebi.ac.uk/pdbsum/1k5q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k5q RCSB]</span>
== 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/k5/1k5q_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=1k5q ConSurf].
<div style="clear:both"></div>


'''PENICILLIN ACYLASE, MUTANT COMPLEXED WITH PAA'''
==See Also==
 
*[[Penicillin acylase|Penicillin acylase]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1K5Q is a [[Protein complex]] structure of sequences 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=1K5Q OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15254299 15254299]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Penicillin amidase]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Dijkstra BW]]
[[Category: Dijkstra, B W.]]
[[Category: Hensgens CMH]]
[[Category: Hensgens, C M.H.]]
[[Category: Keizer E]]
[[Category: Keizer, E.]]
[[Category: Snijder HJ]]
[[Category: Snijder, H J.]]
[[Category: beta-strand]]
[[Category: helice]]
[[Category: ntn-hydrolase fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:43:56 2008''

Latest revision as of 13:25, 13 March 2024

PENICILLIN ACYLASE, MUTANT COMPLEXED WITH PAA

1k5q, resolution 2.34Å

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