1k57: Difference between revisions

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[[Image:1k57.png|left|200px]]


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==OXA 10 class D beta-lactamase at pH 6.0==
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<StructureSection load='1k57' size='340' side='right'caption='[[1k57]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1k57]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K57 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1k57|  PDB=1k57  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k57 OCA], [https://pdbe.org/1k57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k57 RCSB], [https://www.ebi.ac.uk/pdbsum/1k57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k57 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLO10_PSEAI BLO10_PSEAI] Hydrolyzes both carbenicillin and oxacillin.
== 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/k5/1k57_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=1k57 ConSurf].
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== Publication Abstract from PubMed ==
beta-Lactamases are the resistance enzymes for beta-lactam antibiotics, of which four classes are known. beta-lactamases hydrolyze the beta-lactam moieties of these antibiotics, rendering them inactive. It is shown herein that the class D OXA-10 beta-lactamase depends critically on an unusual carbamylated lysine as the basic residue for both the enzyme acylation and deacylation steps of catalysis. The formation of carbamylated lysine is reversible. Evidence is presented that this enzyme is dimeric and carbamylated in living bacteria. High-resolution x-ray structures for the native enzyme were determined at pH values of 6.0, 6.5, 7.5, and 8.5. Two dimers are present per asymmetric unit. One monomer in each dimer was carbamylated at pH 6.0, whereas all four monomers were fully carbamylated at pH 8.5. At the intermediate pH values, one monomer of each dimer was carbamylated, and the other showed a mixture of carbamylated and non-carbamylated lysines. It would appear that, as the pH increased for the sample, additional lysines were "titrated" by carbamylation. A handful of carbamylated lysines are known from protein crystallographic data, all of which have been attributed roles in structural stabilization (mostly as metal ligands) of the proteins. This paper reports a previously unrecognized role for a noncoordinated carbamylate lysine as a basic residue involved in mechanistic reactions of an enzyme, which indicates another means for expansion of the catalytic capabilities of the amino acids in nature beyond the 20 common amino acids in development of biological catalysts.


===OXA 10 class D beta-lactamase at pH 6.0===
Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases.,Golemi D, Maveyraud L, Vakulenko S, Samama JP, Mobashery S Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14280-5. Epub 2001 Nov 27. PMID:11724923<ref>PMID:11724923</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 1k57" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_11724923}}, adds the Publication Abstract to the page
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 11724923 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_11724923}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1K57 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K57 OCA].
 
==Reference==
Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases., Golemi D, Maveyraud L, Vakulenko S, Samama JP, Mobashery S, Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14280-5. Epub 2001 Nov 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11724923 11724923]
[[Category: Beta-lactamase]]
[[Category: Protein complex]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Golemi, D.]]
[[Category: Golemi D]]
[[Category: Maveyraud, L.]]
[[Category: Maveyraud L]]
[[Category: Mobashery, S.]]
[[Category: Mobashery S]]
[[Category: Samama, J P.]]
[[Category: Samama JP]]
[[Category: Vakulenko, S.]]
[[Category: Vakulenko S]]
[[Category: Antibiotic resistance]]
[[Category: Beta-lactamase]]
[[Category: Carbamylation]]
 
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